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Protein

7-alpha-hydroxysteroid dehydrogenase

Gene

hdhA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.

Catalytic activityi

3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD+ = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei146 – 1461Substrate
Active sitei159 – 1591Proton acceptor
Binding sitei163 – 1631NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 4225NAD1 PublicationAdd
BLAST

GO - Molecular functioni

  • cholate 7-alpha-dehydrogenase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • bile acid catabolic process Source: EcoCyc
  • protein homotetramerization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.
ECOL316407:JW1611-MONOMER.
MetaCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.
BRENDAi1.1.1.159. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
7-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.159)
Short name:
7-alpha-HSDH
Gene namesi
Name:hdhA
Synonyms:hsdH
Ordered Locus Names:b1619, JW1611
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10425. hdhA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi146 – 1461S → A or H: Reduces activity by over 65%. 1 Publication
Mutagenesisi159 – 1591Y → F: Loss of activity. 1 Publication
Mutagenesisi159 – 1591Y → H: Reduces activity by 87%. 1 Publication
Mutagenesisi163 – 1631K → I: Reduces activity by 95%. 1 Publication
Mutagenesisi163 – 1631K → R: Reduces activity by 35%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2552557-alpha-hydroxysteroid dehydrogenasePRO_0000054708Add
BLAST

Proteomic databases

PaxDbiP0AET8.
PRIDEiP0AET8.

2D gel databases

SWISS-2DPAGEP0AET8.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259598. 16 interactions.
DIPiDIP-9875N.
IntActiP0AET8. 5 interactions.
STRINGi511145.b1619.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi13 – 164Combined sources
Turni17 – 204Combined sources
Helixi22 – 3211Combined sources
Turni33 – 353Combined sources
Beta strandi37 – 437Combined sources
Helixi45 – 5713Combined sources
Beta strandi62 – 665Combined sources
Helixi72 – 8615Combined sources
Beta strandi91 – 944Combined sources
Helixi108 – 11811Combined sources
Helixi120 – 13617Combined sources
Beta strandi139 – 1446Combined sources
Helixi147 – 1493Combined sources
Helixi157 – 17822Combined sources
Turni179 – 1813Combined sources
Beta strandi182 – 1898Combined sources
Helixi195 – 1984Combined sources
Helixi203 – 2119Combined sources
Helixi221 – 23212Combined sources
Helixi234 – 2363Combined sources
Beta strandi243 – 2475Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHHX-ray2.30A/B1-255[»]
1AHIX-ray2.30A/B1-255[»]
1FMCX-ray1.80A/B1-255[»]
ProteinModelPortaliP0AET8.
SMRiP0AET8. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AET8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107ZQV. Bacteria.
ENOG410XPR5. LUCA.
InParanoidiP0AET8.
KOiK00076.
OMAiVPKHTVY.
OrthoDBiEOG6N3CR8.
PhylomeDBiP0AET8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AET8-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:255
Mass (Da):26,779
Last modified:December 20, 2005 - v1
Checksum:i66CF70E85BD67B6D
GO

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.
PIRiA38527.
RefSeqiNP_416136.1. NC_000913.3.
WP_000483353.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74691; AAC74691; b1619.
BAA15370; BAA15370; BAA15370.
GeneIDi946151.
KEGGiag:BAA01384.
ecj:JW1611.
eco:b1619.
PATRICi32118540. VBIEscCol129921_1690.

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.
PIRiA38527.
RefSeqiNP_416136.1. NC_000913.3.
WP_000483353.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHHX-ray2.30A/B1-255[»]
1AHIX-ray2.30A/B1-255[»]
1FMCX-ray1.80A/B1-255[»]
ProteinModelPortaliP0AET8.
SMRiP0AET8. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259598. 16 interactions.
DIPiDIP-9875N.
IntActiP0AET8. 5 interactions.
STRINGi511145.b1619.

2D gel databases

SWISS-2DPAGEP0AET8.

Proteomic databases

PaxDbiP0AET8.
PRIDEiP0AET8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74691; AAC74691; b1619.
BAA15370; BAA15370; BAA15370.
GeneIDi946151.
KEGGiag:BAA01384.
ecj:JW1611.
eco:b1619.
PATRICi32118540. VBIEscCol129921_1690.

Organism-specific databases

EchoBASEiEB0420.
EcoGeneiEG10425. hdhA.

Phylogenomic databases

eggNOGiENOG4107ZQV. Bacteria.
ENOG410XPR5. LUCA.
InParanoidiP0AET8.
KOiK00076.
OMAiVPKHTVY.
OrthoDBiEOG6N3CR8.
PhylomeDBiP0AET8.

Enzyme and pathway databases

BioCyciEcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.
ECOL316407:JW1611-MONOMER.
MetaCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.
BRENDAi1.1.1.159. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AET8.
PROiP0AET8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Strain: ATCC 33694 / HB101.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Jefferson R.A.
    Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-255.
  6. "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: MUTAGENESIS OF SER-146; TYR-159 AND LYS-163.
  7. "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 COMPLEX WITH SUBSTRATE ANALOG AND NAD.
    Strain: ATCC 33694 / HB101.

Entry informationi

Entry nameiHDHA_ECOLI
AccessioniPrimary (citable) accession number: P0AET8
Secondary accession number(s): P25529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.