7-alpha-hydroxysteroid dehydrogenase - Escherichia coli (strain K12)

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P0AET8 (HDHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
7-alpha-hydroxysteroid dehydrogenase
Short name=7-alpha-HSDH
EC=1.1.1.159

Gene names

Name:	hdhA
Synonyms:	hsdH
Ordered Locus Names:	b1619, JW1611

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.
Catalytic activity	3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD⁺ = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Bile acid catabolism Lipid metabolism Steroid metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	bile acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	cholate 7-alpha-dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 255

255

7-alpha-hydroxysteroid dehydrogenase

PRO_0000054708

Regions

Nucleotide binding

18 – 42

NAD

Sites

Active site

159

Proton acceptor

Binding site

146

Substrate

Binding site

163

NAD

Experimental info

Mutagenesis

146

S → A or H: Reduces activity by over 65%. Ref.6

Mutagenesis

159

Y → F: Loss of activity. Ref.6

Mutagenesis

159

Y → H: Reduces activity by 87%. Ref.6

Mutagenesis

163

K → I: Reduces activity by 95%. Ref.6

Mutagenesis

163

K → R: Reduces activity by 35%. Ref.6

Secondary structure

255

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AET8 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 66CF70E85BD67B6D
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FASTA

255

26,779

        10         20         30         40         50         60 
MFNSDNLRLD GKCAIITGAG AGIGKEIAIT FATAGASVVV SDINADAANH VVDEIQQLGG 

        70         80         90        100        110        120 
QAFACRCDIT SEQELSALAD FAISKLGKVD ILVNNAGGGG PKPFDMPMAD FRRAYELNVF 

       130        140        150        160        170        180 
SFFHLSQLVA PEMEKNGGGV ILTITSMAAE NKNINMTSYA SSKAAASHLV RNMAFDLGEK 

       190        200        210        220        230        240 
NIRVNGIAPG AILTDALKSV ITPEIEQKML QHTPIRRLGQ PQDIANAALF LCSPAASWVS 

       250 
GQILTVSGGG VQELN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2007545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 33694 / HB101.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9722677] [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: 8672472] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND NAD. Strain: ATCC 33694 / HB101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10497 Genomic DNA. Translation: BAA01384.1.
U00096 Genomic DNA. Translation: AAC74691.1.
AP009048 Genomic DNA. Translation: BAA15370.1.
M14641 Genomic DNA. Translation: AAA68921.1.

PIR

A38527.

RefSeq

NP_416136.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AET8.

SMR

P0AET8. Positions 1-255.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AET8. 7 interactions.

2D gel databases

SWISS-2DPAGE

P0AET8.

2DBase-Ecoli

P0AET8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004241; EBESCP00000004241; EBESCG00000003459.
EBESCT00000014247; EBESCP00000013538; EBESCG00000013309.

GeneID

946151.

GenomeReviews

Gene locus JW1611 in contig AP009048_GR.
Gene locus b1619 in contig U00096_GR.

KEGG

ecj:JW1611.
eco:b1619.

PATRIC

32118540. VBIEscCol129921_1690.

Organism-specific databases

EchoBASE

EB0420.

EcoGene

EG10425. hdhA.

Phylogenomic databases

eggNOG

COG1028.

GeneTree

EBGT00050000009180.

HOGENOM

HBG750976.

OMA

WRCDITS.

PhylomeDB

P0AET8.

ProtClustDB

PRK06113.

Enzyme and pathway databases

BioCyc

EcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.
MetaCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER.

Gene expression databases

Genevestigator

P0AET8.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

K00076.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HDHA_ECOLI

Accession

Primary (citable) accession number: P0AET8
Secondary accession number(s): P25529

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents