UniProtKB - O87605 (PIKC_STRVZ)
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>sp|O87605|PIKC_STRVZ Cytochrome P450 monooxygenase PikC OS=Streptomyces venezuelae OX=54571 GN=pikC PE=1 SV=1 MRRTQQGTTASPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDR ARAVLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTMRRVELLR PRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEPDRAAFRVWTDAFVF PDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSALVRTSDEDGSRLTSEELLGMAHIL LVAGHETTVNLIANGMYALLSHPDQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVE PVDLDGTVIPAGDTVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLA RLEARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRRGREAGRRTGCommunity curation ()Add a publicationFeedback
Cytochrome P450 monooxygenase PikC
pikC
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- 2 H+EC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
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- 2 H+EC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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2H+- Search proteins in UniProtKB for this molecule.
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+narbomycin- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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- 4 H+EC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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4H+- Search proteins in UniProtKB for this molecule.
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+narbomycin- Search proteins in UniProtKB for this molecule.
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+2O2- Search proteins in UniProtKB for this molecule.
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+novapikromycin- Search proteins in UniProtKB for this molecule.
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- 10-deoxymethymycinEC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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10-deoxymethymycin- Search proteins in UniProtKB for this molecule.
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+2H+- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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+2reduced [2Fe-2S]-[ferredoxin]- Search proteins in UniProtKB for this molecule.
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=H2O- Search proteins in UniProtKB for this molecule.
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+methymycin- Search proteins in UniProtKB for this molecule.
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+2oxidized [2Fe-2S]-[ferredoxin]- Search proteins in UniProtKB for this molecule.
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- 10-deoxymethymycinEC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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10-deoxymethymycin- Search proteins in UniProtKB for this molecule.
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+2H+- Search proteins in UniProtKB for this molecule.
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+O2- Search proteins in UniProtKB for this molecule.
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+2reduced [2Fe-2S]-[ferredoxin]- Search proteins in UniProtKB for this molecule.
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=H2O- Search proteins in UniProtKB for this molecule.
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+neomethymycin- Search proteins in UniProtKB for this molecule.
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- 10-deoxymethymycinEC:1.14.15.33
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Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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10-deoxymethymycin- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=120 µM for narbomycin1 Publication
Manual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
- KM=20.4 µM for 10-deoxymethymycin1 Publication
Manual assertion based on experiment ini
- Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=44 µM for narbomycin1 Publication
Manual assertion based on experiment ini
- Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Antibiotic biosynthesis
This protein is involved in Antibiotic biosynthesis.7 PublicationsManual assertion based on experiment ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity."
Xue Y., Zhao L., Liu H.W., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, PATHWAY, DISRUPTION PHENOTYPE. - Ref.4"The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae."
Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., Podust L.M.
J. Biol. Chem. 281:26289-26297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94. - Ref.6"Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase."
Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY. - Ref.7"Directing group-controlled regioselectivity in an enzymatic C-H bond oxygenation."
Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L., Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.
J. Am. Chem. Soc. 136:4901-4904(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 94 | Substrate2 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 354 | Iron (heme axial ligand)4 Publications Manual assertion based on experiment ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- heme binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
- iron ion binding Source: UniProtKBInferred from direct assayi
- Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
- monooxygenase activity Source: UniProtKBInferred from direct assayi
- Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro
GO - Biological processi
- macrolide biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
- oxidation-reduction process Source: UniProtKBInferred from direct assayi
- Ref.5"Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae."
Li S., Ouellet H., Sherman D.H., Podust L.M.
J. Biol. Chem. 284:5723-5730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Antibiotic biosynthesis |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-18405 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.13.185, 6106 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Cytochrome P450 monooxygenase PikC1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Alternative name(s): Cytochrome P450 monooxygenase PicK1 Publication Manual assertion based on opinion ini
Narbomycin C-12 hydroxylase1 Publication Manual assertion based on opinion ini
Pikromycin synthase CYP107L1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:pikC2 Publications Manual assertion based on opinion ini
Synonyms:picK1 Publication Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Streptomyces venezuelaeImported Manual assertion inferred from database entriesi |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 54571 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces |
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Manual assertion based on experiment ini
- Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.3"A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity."
Xue Y., Zhao L., Liu H.W., Sherman D.H.
Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, PATHWAY, DISRUPTION PHENOTYPE.
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 50 | D → A: Mildly reduces activity with YC-17 and narbomycin. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 50 | D → N: Increases affinity for narbomycin and YC-17. Mildly increases activity YC-17 and narbomycin. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 85 | E → A: Strongly reduces activity with narbomycin, but has only minor effect on activity with YC-17. Loss of activity with YC-17 and narbomycin; when associated with A-94. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 85 | E → Q: Reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 94 | E → A: Strongly reduces activity with YC-17, but has only minor effect on activity with narbomycin. Loss of activity with YC-17 and narbomycin; when associated with A-85. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 94 | E → Q: Strongly reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000430718 | 1 – 416 | Cytochrome P450 monooxygenase PikCAdd BLAST | 416 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 14 – 16 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 18 – 20 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 21 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 29 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 40 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 47 – 49 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 51 – 55 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 58 – 65 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 74 – 76 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 83 – 88 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 92 – 94 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 99 – 107 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 108 – 111 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 113 – 117 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 120 – 135 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
Beta strandi | 137 – 139 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 140 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 144 – 147 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 148 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 151 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 165 – 167 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 170 – 179 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 184 – 205 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
Helixi | 213 – 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Turni | 225 – 227 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 230 – 243 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 246 – 261 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
Helixi | 263 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 273 – 275 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 276 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 289 – 292 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 296 – 300 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 302 – 304 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 307 – 309 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 315 – 317 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 319 – 322 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 326 – 328 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 329 – 331 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 350 – 353 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 357 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
Beta strandi | 379 – 382 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 384 – 386 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 393 – 395 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 402 – 404 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O87605 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O87605 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 187 – 191 | Substrate binding2 Publications Manual assertion based on experiment ini
| 5 | |
Regioni | 238 – 246 | Substrate binding2 Publications Manual assertion based on experiment ini
| 9 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Manual assertion based on opinion ini
- Ref.1"Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin."
Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.
Biochemistry 37:14937-14942(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY. - Ref.2"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae."
Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.
Chem. Biol. 5:661-667(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
CuratedFamily and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.630.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001128, Cyt_P450 IPR002397, Cyt_P450_B IPR017972, Cyt_P450_CS IPR036396, Cyt_P450_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00067, p450, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00359, BP450 PR00385, P450 |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48264, SSF48264, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MRRTQQGTTA SPPVLDLGAL GQDFAADPYP TYARLRAEGP AHRVRTPEGD
60 70 80 90 100
EVWLVVGYDR ARAVLADPRF SKDWRNSTTP LTEAEAALNH NMLESDPPRH
110 120 130 140 150
TRLRKLVARE FTMRRVELLR PRVQEIVDGL VDAMLAAPDG RADLMESLAW
160 170 180 190 200
PLPITVISEL LGVPEPDRAA FRVWTDAFVF PDDPAQAQTA MAEMSGYLSR
210 220 230 240 250
LIDSKRGQDG EDLLSALVRT SDEDGSRLTS EELLGMAHIL LVAGHETTVN
260 270 280 290 300
LIANGMYALL SHPDQLAALR ADMTLLDGAV EEMLRYEGPV ESATYRFPVE
310 320 330 340 350
PVDLDGTVIP AGDTVLVVLA DAHRTPERFP DPHRFDIRRD TAGHLAFGHG
360 370 380 390 400
IHFCIGAPLA RLEARIAVRA LLERCPDLAL DVSPGELVWY PNPMIRGLKA
410
LPIRWRRGRE AGRRTG
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF087022 Genomic DNA Translation: AAC64105.1 AF079139 Genomic DNA Translation: AAC68886.1 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:AAC68886 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
O87605 | Cytochrome P450 | 416 | UniRef90_O87605 | |||
Cytochrome P450 | 415 | |||||
Cytochrome | 415 | |||||
Cytochrome P450 | 408 | |||||
+6 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
O87605 | Cytochrome P450 | 416 | UniRef50_O87605 | |||
Cytochrome | 415 | |||||
Cytochrome P450 | 415 | |||||
Cytochrome P450 | 408 | |||||
Cytochrome | 393 | |||||
+761 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF087022 Genomic DNA Translation: AAC64105.1 AF079139 Genomic DNA Translation: AAC68886.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2BVJ | X-ray | 2.10 | A/B | 1-416 | [»] | |
2C6H | X-ray | 2.35 | A/B | 1-416 | [»] | |
2C7X | X-ray | 1.75 | A | 1-416 | [»] | |
2CA0 | X-ray | 2.85 | A/B | 1-416 | [»] | |
2CD8 | X-ray | 1.70 | A/B | 1-416 | [»] | |
2VZ7 | X-ray | 3.20 | A/B | 1-416 | [»] | |
2VZM | X-ray | 1.85 | A/B | 1-416 | [»] | |
2WHW | X-ray | 2.20 | A/B | 1-416 | [»] | |
2WI9 | X-ray | 2.00 | A/B | 1-416 | [»] | |
3ZK5 | X-ray | 1.89 | A/B | 1-416 | [»] | |
3ZPI | X-ray | 1.63 | A/B | 1-416 | [»] | |
4B7D | X-ray | 1.89 | A/B | 1-416 | [»] | |
4B7S | X-ray | 1.84 | A/B | 1-416 | [»] | |
4BF4 | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P | 1-416 | [»] | |
4UMZ | X-ray | 2.32 | A/B | 1-416 | [»] | |
SMRi | O87605 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
KEGGi | ag:AAC68886 |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-18405 |
BRENDAi | 1.14.13.185, 6106 |
Miscellaneous databases
EvolutionaryTracei | O87605 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit |
InterProi | View protein in InterPro IPR001128, Cyt_P450 IPR002397, Cyt_P450_B IPR017972, Cyt_P450_CS IPR036396, Cyt_P450_sf |
Pfami | View protein in Pfam PF00067, p450, 1 hit |
PRINTSi | PR00359, BP450 PR00385, P450 |
SUPFAMi | SSF48264, SSF48264, 1 hit |
PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PIKC_STRVZ | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | O87605Primary (citable) accession number: O87605 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 29, 2014 |
Last sequence update: | November 1, 1998 | |
Last modified: | December 2, 2020 | |
This is version 106 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families