UniProtKB - P9WP65 (CPDA_MYCTU)
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>sp|P9WP65|CPDA_MYCTU 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=cpdA PE=1 SV=1 MHRLRAAEHPRPDYVLLHISDTHLIGGDRRLYGAVDADDRLGELLEQLNQSGLRPDAIVF TGDLADKGEPAAYRKLRGLVEPFAAQLGAELVWVMGNHDDRAELRKFLLDEAPSMAPLDR VCMIDGLRIIVLDTSVPGHHHGEIRASQLGWLAEELATPAPDGTILALHHPPIPSVLDMA VTVELRDQAALGRVLRGTDVRAILAGHLHYSTNATFVGIPVSVASATCYTQDLTVAAGGT RGRDGAQGCNLVHVYPDTVVHSVIPLGGGETVGTFVSPGQARRKIAESGIFIEPSRRDSL FKHPPMVLTSSAPRSPVDCommunity curation ()Add a publicationFeedback
Protein
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
Gene
cpdA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:
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
Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Can also hydrolyze cGMP, p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)), p-nitrophenyl phenylphosphonate (pNPPP) and 2',3'-cAMP. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall.UniRule annotation
<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
2 Publications<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.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
<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
- 3',5'-cyclic AMPEC:3.1.4.53
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Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
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Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Source: Rhea- Search for this reaction in UniProtKB.
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3',5'-cyclic AMP- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=AMP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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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
Protein has several cofactor binding sites:- Fe3+
- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Manual assertion based on experiment ini
- Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Mn2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Manual assertion based on experiment ini
- Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Enhanced by magnesium or manganese. Activity decreases in the presence of orthovanadate and phosphotyrosine.1 Publication
Manual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING.
<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=5.5 mM for 3',5'-cAMP1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- KM=0.9 mM for bis(pNPP)1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- KM=0.9 mM for pNPPP1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- KM=1 mM for 2',3'-cAMP1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Vmax=1.1 µmol/min/mg enzyme with 3',5'-cAMP as substrate1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Vmax=74 µmol/min/mg enzyme with bis(pNPP) as substrate1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Vmax=112.7 µmol/min/mg enzyme with pNPPP as substrate1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Vmax=14.7 µmol/min/mg enzyme with 2',3'-cAMP as substrate1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Vmax=0.017 µmol/min/mg enzyme with pNPP as substrate1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
pH dependencei
Optimum pH is 8.5-9.5.1 Publication
Manual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING.
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 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 | 21 | Iron2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 23 | Iron2 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 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 | 23 | cAMPUniRule annotation Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 63 | Iron2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 63 | Manganese2 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 63 | cAMPUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 97 | Manganese2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 169 | Manganese2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 207 | Manganese2 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 209 | Iron2 Publications Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 209 | cAMPUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 |
Regions
| 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 a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 97 – 98 | cAMPUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 2 |
<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
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Source: MTBBASE
<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"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- 3',5'-cyclic-AMP phosphodiesterase activity Source: MTBBASEInferred from direct assayi
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - "A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity."
Keppetipola N., Shuman S.
J Biol Chem 283:30942-30949(2008) [PubMed] [Europe PMC] [Abstract] - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- ferric iron binding Source: MTBBASEInferred from direct assayi
- Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140.
- iron ion binding Source: MTBBASEInferred from direct assayi
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- manganese ion binding Source: MTBBASEInferred from direct assayi
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- nucleotide binding Source: UniProtKB-UniRule
- phosphatase activity Source: MTBBASEInferred from direct assayi
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- phosphate ion binding Source: MTBBASEInferred from direct assayi
- Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140.
GO - Biological processi
- cAMP catabolic process Source: MTBBASEInferred from direct assayi
- "Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase."
Agarwal N., Lamichhane G., Gupta R., Nolan S., Bishai W.R.
Nature 460:98-102(2009) [PubMed] [Europe PMC] [Abstract] - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- cell wall modification Source: MTBBASEInferred from direct assayi
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- pathogenesis Source: MTBBASE
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Murine model to study the invasion and survival of Mycobacterium tuberculosis in the central nervous system."
Be N.A., Lamichhane G., Grosset J., Tyagi S., Cheng Q.J., Kim K.S., Bishai W.R., Jain S.K.
J Infect Dis 198:1520-1528(2008) [PubMed] [Europe PMC] [Abstract]
<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 | Hydrolase |
| Ligand | cAMP, Iron, Manganese, Metal-binding, Nucleotide-binding |
<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: 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAUniRule annotationManual assertion according to rulesi (EC:3.1.4.53
Manual assertion according to rulesi )Short name: 3',5'-cyclic AMP phosphodiesteraseUniRule annotation Manual assertion according to rulesi Short name: cAMP phosphodiesteraseUniRule annotation Manual assertion according to rulesi |
| <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:cpdAUniRule annotation Manual assertion according to rulesi Synonyms:icc Ordered Locus Names:Rv0805 |
| <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 | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| <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 | 83332 [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 › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium tuberculosis |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Mycobacterium tuberculosis strain H37Rv genome database More...TubercuListi | Rv0805 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cytoplasm 1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- Cell membrane 1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- cell wall 1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Note: Localization to the cell membrane and cell wall could be due to a specialized secretion system operative in mycobacteria.1 Publication - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Manual assertion inferred by curator fromi
GO - Cellular componenti
- cell wall Source: MTBBASEInferred from direct assayi
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
- cytoplasm Source: UniProtKB-SubCell
- extracellular region Source: UniProtKB-KW
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, Cell wall, Cytoplasm, Membrane, Secreted<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
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 | 21 | D → A: 90% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 23 | H → A: 50% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 66 | D → A: 25% decrease in bis(pNPP) hydrolysis. 70% decrease in cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 97 | N → A: Loss of bis(pNPP) and 3',5'-cAMP hydrolysis. Strong decrease in 2',3'-cAMP hydrolysis. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 98 | H → A: 40% decrease in bis(pNPP) hydrolysis. Strong decrease in 3',5'-cAMP and 2',3'-cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 140 | H → A: No change in activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 169 | H → A: 50% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 207 | H → A: 75% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 209 | H → A: 80% decrease in hydrolysis of 3',5'-cAMP and bis(pNPP). 40% decrease in 2',3'-cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 229 | Y → A: 40% decrease in bis(pNPP) hydrolysis. 80% decrease in 3',5'-cAMP and 2',3'-cAMP hydrolysis. 1 Publication Manual assertion based on experiment ini
| 1 |
Miscellaneous databases
Pathogen-Host Interaction database More...PHI-basei | PHI:4238 |
<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_0000413370 | 1 – 318 | 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAAdd BLAST | 318 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P9WP65 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
3 PublicationsManual assertion based on experiment ini
- Ref.2"The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis."
Shenoy A.R., Sreenath N., Podobnik M., Kovacevic M., Visweswariah S.S.
Biochemistry 44:15695-15704(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-21; HIS-23; ASP-66; ASN-97; HIS-169 AND HIS-207, HOMOLOGY MODELING. - Ref.4"Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis."
Shenoy A.R., Capuder M., Draskovic P., Lamba D., Visweswariah S.S., Podobnik M.
J. Mol. Biol. 365:211-225(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 3-278 OF WILD-TYPE; MUTANT ALA-66 AND MUTANT ALA-97 IN COMPLEXES WITH IRON AND MANGANESE, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-140. - Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 83332.Rv0805 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| 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 | 13 – 19 | 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 | 7 | |
| Beta strandi | 26 – 28 | Combined sources 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 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 | 32 – 34 | Combined sources 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 | 37 – 51 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 56 – 60 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 65 – 67 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 70 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| Beta strandi | 90 – 93 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 101 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 120 – 124 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 127 – 131 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 140 – 142 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 146 – 155 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 164 – 167 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 178 – 183 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 184 – 186 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 188 – 195 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 198 – 205 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 207 – 210 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 212 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 219 – 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 242 – 244 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 248 – 254 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 259 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 278 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P9WP65 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<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
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The C-terminal domain is used to better adjust the substrates into the active sites and to facilitate subcellular localization of the protein.1 Publication
Manual assertion based on experiment ini
- Ref.5"A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability."
Podobnik M., Tyagi R., Matange N., Dermol U., Gupta A.K., Mattoo R., Seshadri K., Visweswariah S.S.
J. Biol. Chem. 284:32846-32857(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-318 IN COMPLEX WITH IRON; MANGANESE AND AMP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASN-97; HIS-98; HIS-140; HIS-209 AND TYR-229.
<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
Belongs to the cAMP phosphodiesterase class-III family.UniRule annotation
Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1409, Bacteria |
Identification of Orthologs from Complete Genome Data More...OMAi | CAWLDQH |
Database for complete collections of gene phylogenies More...PhylomeDBi | P9WP65 |
Family and domain databases
Conserved Domains Database More...CDDi | cd07402, MPP_GpdQ, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.21.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00905, cAMP_phosphodiest_CpdA, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004843, Calcineurin-like_PHP_ApaH IPR026575, cAMP_Pdiest_CpdA IPR029052, Metallo-depent_PP-like |
Pfam protein domain database More...Pfami | View protein in Pfam PF00149, Metallophos, 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.
P9WP65-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MHRLRAAEHP RPDYVLLHIS DTHLIGGDRR LYGAVDADDR LGELLEQLNQ
60 70 80 90 100
SGLRPDAIVF TGDLADKGEP AAYRKLRGLV EPFAAQLGAE LVWVMGNHDD
110 120 130 140 150
RAELRKFLLD EAPSMAPLDR VCMIDGLRII VLDTSVPGHH HGEIRASQLG
160 170 180 190 200
WLAEELATPA PDGTILALHH PPIPSVLDMA VTVELRDQAA LGRVLRGTDV
210 220 230 240 250
RAILAGHLHY STNATFVGIP VSVASATCYT QDLTVAAGGT RGRDGAQGCN
260 270 280 290 300
LVHVYPDTVV HSVIPLGGGE TVGTFVSPGQ ARRKIAESGI FIEPSRRDSL
310
FKHPPMVLTS SAPRSPVD
Length:318
Mass (Da):34,233
Last modified:April 16, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i7C1B683C5E375B3F
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 | AL123456 Genomic DNA Translation: CCP43553.1 |
Protein sequence database of the Protein Information Resource More...PIRi | F70536 |
NCBI Reference Sequences More...RefSeqi | NP_215320.1, NC_000962.3 WP_003404120.1, NZ_NVQJ01000064.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | CCP43553; CCP43553; Rv0805 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 885326 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mtu:Rv0805 |
<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
<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 | AL123456 Genomic DNA Translation: CCP43553.1 |
| PIRi | F70536 |
| RefSeqi | NP_215320.1, NC_000962.3 WP_003404120.1, NZ_NVQJ01000064.1 |
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 |
| 2HY1 | X-ray | 1.93 | A | 3-278 | [»] | |
| 2HYO | X-ray | 2.25 | A | 3-278 | [»] | |
| 2HYP | X-ray | 2.05 | A | 3-278 | [»] | |
| 3IB7 | X-ray | 1.60 | A | 2-318 | [»] | |
| 3IB8 | X-ray | 1.80 | A | 2-318 | [»] | |
| SMRi | P9WP65 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 83332.Rv0805 |
Proteomic databases
| PaxDbi | P9WP65 |
Genome annotation databases
| EnsemblBacteriai | CCP43553; CCP43553; Rv0805 |
| GeneIDi | 885326 |
| KEGGi | mtu:Rv0805 |
Organism-specific databases
| TubercuListi | Rv0805 |
Phylogenomic databases
| eggNOGi | COG1409, Bacteria |
| OMAi | CAWLDQH |
| PhylomeDBi | P9WP65 |
Miscellaneous databases
| PHI-basei | PHI:4238 |
Family and domain databases
| CDDi | cd07402, MPP_GpdQ, 1 hit |
| Gene3Di | 3.60.21.10, 1 hit |
| HAMAPi | MF_00905, cAMP_phosphodiest_CpdA, 1 hit |
| InterProi | View protein in InterPro IPR004843, Calcineurin-like_PHP_ApaH IPR026575, cAMP_Pdiest_CpdA IPR029052, Metallo-depent_PP-like |
| Pfami | View protein in Pfam PF00149, Metallophos, 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 | CPDA_MYCTU | |
| <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 | P9WP65Primary (citable) accession number: P9WP65 Secondary accession number(s): L0T7J7, O06629, Q7D993 | |
| <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: | April 16, 2014 |
| Last sequence update: | April 16, 2014 | |
| Last modified: | February 10, 2021 | |
| This is version 40 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-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
