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Protein

7-alpha-hydroxysteroid dehydrogenase

Gene

hdhA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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
  • lipid catabolic process Source: UniProtKB-KW
  • protein homotetramerization Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
Biological processBile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism
LigandNAD

Enzyme and pathway databases

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

Chemistry databases

SwissLipidsiSLP:000001736

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: EcoCyc

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

Chemistry databases

DrugBankiDB02123 Glycochenodeoxycholic Acid

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiP0AET8
PRIDEiP0AET8

2D gel databases

SWISS-2DPAGEiP0AET8

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259598, 31 interactors
DIPiDIP-9875N
IntActiP0AET8, 5 interactors
STRINGi316385.ECDH10B_1752

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
OMAiINVHGAF
PhylomeDBiP0AET8

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

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
PATRICifig|1411691.4.peg.642

Similar proteinsi

Entry informationi

Entry nameiHDHA_ECOLI
AccessioniPrimary (citable) accession number: P0AET8
Secondary accession number(s): P25529
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 108 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health