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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)DescriptionActionsGraphical viewLength
Binding sitei146Substrate1
Active sitei159Proton acceptor1
Binding sitei163NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 42NAD1 PublicationAdd BLAST25

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi146S → A or H: Reduces activity by over 65%. 1 Publication1
Mutagenesisi159Y → F: Loss of activity. 1 Publication1
Mutagenesisi159Y → H: Reduces activity by 87%. 1 Publication1
Mutagenesisi163K → I: Reduces activity by 95%. 1 Publication1
Mutagenesisi163K → R: Reduces activity by 35%. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000547081 – 2557-alpha-hydroxysteroid dehydrogenaseAdd BLAST255

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 interactors.
DIPiDIP-9875N.
IntActiP0AET8. 5 interactors.
STRINGi511145.b1619.

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Beta strandi13 – 16Combined sources4
Turni17 – 20Combined sources4
Helixi22 – 32Combined sources11
Turni33 – 35Combined sources3
Beta strandi37 – 43Combined sources7
Helixi45 – 57Combined sources13
Beta strandi62 – 66Combined sources5
Helixi72 – 86Combined sources15
Beta strandi91 – 94Combined sources4
Helixi108 – 118Combined sources11
Helixi120 – 136Combined sources17
Beta strandi139 – 144Combined sources6
Helixi147 – 149Combined sources3
Helixi157 – 178Combined sources22
Turni179 – 181Combined sources3
Beta strandi182 – 189Combined sources8
Helixi195 – 198Combined sources4
Helixi203 – 211Combined sources9
Helixi221 – 232Combined sources12
Helixi234 – 236Combined sources3
Beta strandi243 – 247Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AET8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107ZQV. Bacteria.
ENOG410XPR5. LUCA.
InParanoidiP0AET8.
KOiK00076.
OMAiTHDWWNA.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AHHX-ray2.30A/B1-255[»]
1AHIX-ray2.30A/B1-255[»]
1FMCX-ray1.80A/B1-255[»]
ProteinModelPortaliP0AET8.
SMRiP0AET8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259598. 16 interactors.
DIPiDIP-9875N.
IntActiP0AET8. 5 interactors.
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.
OMAiTHDWWNA.
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...

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: November 2, 2016
This is version 98 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.