UniProtKB - P0AET8 (HDHA_ECOLI)
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>sp|P0AET8|HDHA_ECOLI 7alpha-hydroxysteroid dehydrogenase OS=Escherichia coli (strain K12) OX=83333 GN=hdhA PE=1 SV=1 MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGG QAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVF SFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEK NIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVS GQILTVSGGGVQELNCommunity curation ()Add a publicationFeedback
7alpha-hydroxysteroid dehydrogenase
hdhA
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
7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD+-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7-oxosteroids. To a lesser extent, can also act on taurochenodeoxycholate, taurocholate and glycocholate (PubMed:2007545).
Can also use glycochenodeoxycholate as substrate (PubMed:8672472).
Is not able to use NADP+ instead of NAD+ as the electron acceptor (PubMed:2007545).
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.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT. - Ref.6"Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.
Biochemistry 35:7715-7730(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE.
<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
- cholateEC:1.1.1.159
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT. - Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT. - Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
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<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
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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cholate- Search proteins in UniProtKB for this molecule.
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=3α,12α-dihydroxy-7-oxo-5β-cholanate- Search proteins in UniProtKB for this molecule.
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+NADH- Search proteins in UniProtKB for this molecule.
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- chenodeoxycholate
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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Manual assertion inferred by curator fromi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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chenodeoxycholate- Search proteins in UniProtKB for this molecule.
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=7-oxolithocholate- Search proteins in UniProtKB for this molecule.
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- NAD+
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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Manual assertion inferred by curator fromi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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NAD+- Search proteins in UniProtKB for this molecule.
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+taurochenodeoxycholate- Search proteins in UniProtKB for this molecule.
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=7-oxotaurolithocholate- Search proteins in UniProtKB for this molecule.
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+NADH- Search proteins in UniProtKB for this molecule.
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- NAD+
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion inferred by curator fromi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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NAD+- Search proteins in UniProtKB for this molecule.
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+taurocholate- Search proteins in UniProtKB for this molecule.
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=7-oxo-taurodeoxycholate- Search proteins in UniProtKB for this molecule.
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+NADH- Search proteins in UniProtKB for this molecule.
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- glycocholate
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Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion inferred by curator fromi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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glycocholate- Search proteins in UniProtKB for this molecule.
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=7-oxo-glycodeoxycholate- Search proteins in UniProtKB for this molecule.
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+NADH- Search proteins in UniProtKB for this molecule.
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- glycochenodeoxycholate
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Manual assertion based on experiment ini
- Ref.6"Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.
Biochemistry 35:7715-7730(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE.
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Manual assertion inferred by curator fromi
- Ref.6"Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.
Biochemistry 35:7715-7730(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE.
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glycochenodeoxycholate- Search proteins in UniProtKB for this molecule.
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+NAD+- Search proteins in UniProtKB for this molecule.
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=7-oxoglycolithocholate- Search proteins in UniProtKB for this molecule.
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<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
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
<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
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT. - Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
- KM=0.19 mM for taurochenodeoxycholate1 Publication
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- KM=0.43 mM for chenodeoxycholate1 Publication
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- KM=1.2 mM for cholate1 Publication
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- KM=1.25 mM for glycocholate1 Publication
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- KM=2.0 mM for taurocholate1 Publication
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- KM=0.279 mM for NAD+1 Publication
Manual assertion based on experiment ini
- Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
- KM=0.361 mM for cholate1 Publication
Manual assertion based on experiment ini
- Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
pH dependencei
Manual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
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 | 23 | NAD; via amide nitrogenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 95 | NAD; via carbonyl oxygenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 99 | Glycochenodeoxycholate; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 146 | GlycochenodeoxycholateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 146 | Transition state stabilizer2 Publications Manual assertion inferred by curator fromi
| 1 | |
Binding sitei | 151 | GlycochenodeoxycholateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 159 | Proton acceptor2 Publications Manual assertion inferred by curator fromi
| 1 | |
Binding sitei | 159 | GlycochenodeoxycholateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 159 | NADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 163 | NADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Sitei | 163 | Lowers pKa of active site Tyr2 Publications Manual 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 | 42 – 43 | NADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 2 | |
Nucleotide bindingi | 68 – 69 | NADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 2 | |
Nucleotide bindingi | 192 – 194 | NADCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 3 |
<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
- chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity Source: RHEA
- cholate 7-alpha-dehydrogenase activity 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-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.7"Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T.
J. Biochem. 124:634-641(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159; HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, ACTIVE SITE.
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- NAD binding Source: UniProtKBInferred from direct assayi
- Ref.6"Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.
Biochemistry 35:7715-7730(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE.
GO - Biological processi
- bile acid catabolic process Source: EcoCycInferred from direct assayi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- lipid catabolic process Source: UniProtKB-KW
<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 | Oxidoreductase |
Biological process | Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism |
Ligand | NAD |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.159, 2026 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001736 |
<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: 7alpha-hydroxysteroid dehydrogenase1 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
Short name: 7alpha-HSDH1 Publication Manual assertion based on opinion ini
Alternative name(s): NAD-dependent 7alpha-hydroxysteroid dehydrogenase1 Publication Manual assertion inferred by curator fromi
|
<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:hdhA Synonyms:hsdH1 Publication Manual assertion based on opinion ini
Ordered Locus Names:b1619, JW1611 |
<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 | Escherichia coli (strain K12) |
<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 | 83333 [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 › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
<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 |
|
<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
Cytosol
- cytosol Source: EcoCycInferred from direct assayi
- "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract] - "Protein abundance profiling of the Escherichia coli cytosol."
Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
- cytosol Source: EcoCycInferred from direct assayi
Other locations
- protein-containing complex Source: EcoCycInferred from direct assayi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
- protein-containing complex Source: EcoCycInferred from direct assayi
<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 | 146 | S → A or H: Reduction of the catalytic efficiency by over 65%. No effect on the affinity for cholate and NAD. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 159 | Y → F: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 159 | Y → H: Reduction of the catalytic efficiency by 87.7%. No effect on the affinity for cholate and NAD. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 163 | K → I: Reduction of the catalytic efficiency by 95%. No effect on the affinity for cholate and NAD. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 163 | K → R: Reduction of the catalytic efficiency by 35%. No effect on the affinity for cholate and NAD. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB02123, Glycochenodeoxycholic Acid |
<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_0000054708 | 1 – 255 | 7alpha-hydroxysteroid dehydrogenaseAdd BLAST | 255 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P0AET8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AET8 |
PRoteomics IDEntifications database More...PRIDEi | P0AET8 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P0AET8 |
<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
Homotetramer.
2 PublicationsManual assertion based on experiment ini
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT. - Ref.6"Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli."
Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.
Biochemistry 35:7715-7730(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, REACTION MECHANISM, ACTIVE SITE.
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.1"Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme."
Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H., Kurazono K., Tsuru D.
J. Bacteriol. 173:2173-2179(1991) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4259598, 31 interactors |
Database of interacting proteins More...DIPi | DIP-9875N |
Protein interaction database and analysis system More...IntActi | P0AET8, 5 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b1619 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 4 – 7 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 13 – 16 | Combined sources Automatic 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 | 17 – 20 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 22 – 32 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Turni | 33 – 35 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 37 – 43 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 45 – 57 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 62 – 66 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 72 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
Beta strandi | 91 – 94 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 108 – 118 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 120 – 136 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 139 – 144 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 147 – 149 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 157 – 178 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 22 | |
Turni | 179 – 181 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 182 – 189 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 195 – 198 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 203 – 211 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 221 – 232 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 234 – 236 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 243 – 247 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AET8 |
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 | P0AET8 |
<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1028, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_010194_1_3_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AET8 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AET8 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 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
MFNSDNLRLD GKCAIITGAG AGIGKEIAIT FATAGASVVV SDINADAANH
60 70 80 90 100
VVDEIQQLGG QAFACRCDIT SEQELSALAD FAISKLGKVD ILVNNAGGGG
110 120 130 140 150
PKPFDMPMAD FRRAYELNVF SFFHLSQLVA PEMEKNGGGV ILTITSMAAE
160 170 180 190 200
NKNINMTSYA SSKAAASHLV RNMAFDLGEK NIRVNGIAPG AILTDALKSV
210 220 230 240 250
ITPEIEQKML QHTPIRRLGQ PQDIANAALF LCSPAASWVS GQILTVSGGG
VQELN
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 | D10497 Genomic DNA Translation: BAA01384.1 U00096 Genomic DNA Translation: AAC74691.1 AP009048 Genomic DNA Translation: BAA15370.1 M14641 Genomic DNA Translation: AAA68921.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A38527 |
NCBI Reference Sequences More...RefSeqi | NP_416136.1, NC_000913.3 WP_000483353.1, NZ_STEB01000003.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC74691; AAC74691; b1619 BAA15370; BAA15370; BAA15370 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 946151 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:BAA01384 ecj:JW1611 eco:b1619 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.642 |
<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 | |
---|---|---|---|---|---|---|
P0AET8 | 7alpha-hydroxysteroid dehydrogenase | 255 | UniRef100_P0AET9 | |||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
+47 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AET8 | 7alpha-hydroxysteroid dehydrogenase | 255 | UniRef90_P0AET9 | |||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
+775 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AET8 | 7alpha-hydroxysteroid dehydrogenase | 255 | UniRef50_P0AET9 | |||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
7-alpha-hydroxysteroid dehydrogenase | 255 | |||||
+962 |
<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 | D10497 Genomic DNA Translation: BAA01384.1 U00096 Genomic DNA Translation: AAC74691.1 AP009048 Genomic DNA Translation: BAA15370.1 M14641 Genomic DNA Translation: AAA68921.1 |
PIRi | A38527 |
RefSeqi | NP_416136.1, NC_000913.3 WP_000483353.1, NZ_STEB01000003.1 |
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 |
1AHH | X-ray | 2.30 | A/B | 1-255 | [»] | |
1AHI | X-ray | 2.30 | A/B | 1-255 | [»] | |
1FMC | X-ray | 1.80 | A/B | 1-255 | [»] | |
7ENY | X-ray | 2.70 | A/B/C/D/E/F/G/H | 1-255 | [»] | |
SMRi | P0AET8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259598, 31 interactors |
DIPi | DIP-9875N |
IntActi | P0AET8, 5 interactors |
STRINGi | 511145.b1619 |
Chemistry databases
DrugBanki | DB02123, Glycochenodeoxycholic Acid |
SwissLipidsi | SLP:000001736 |
2D gel databases
SWISS-2DPAGEi | P0AET8 |
Proteomic databases
jPOSTi | P0AET8 |
PaxDbi | P0AET8 |
PRIDEi | P0AET8 |
Genome annotation databases
EnsemblBacteriai | AAC74691; AAC74691; b1619 BAA15370; BAA15370; BAA15370 |
GeneIDi | 946151 |
KEGGi | ag:BAA01384 ecj:JW1611 eco:b1619 |
PATRICi | fig|1411691.4.peg.642 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0420 |
Phylogenomic databases
eggNOGi | COG1028, Bacteria |
HOGENOMi | CLU_010194_1_3_6 |
InParanoidi | P0AET8 |
PhylomeDBi | P0AET8 |
Enzyme and pathway databases
BioCyci | EcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER |
BRENDAi | 1.1.1.159, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0AET8 |
Protein Ontology More...PROi | PR:P0AET8 |
Family and domain databases
InterProi | View protein in InterPro IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
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 | HDHA_ECOLI | |
<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 | P0AET8Primary (citable) accession number: P0AET8 Secondary accession number(s): P25529 | |
<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: | December 20, 2005 |
Last sequence update: | December 20, 2005 | |
Last modified: | February 23, 2022 | |
This is version 127 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, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families