Reviewed, UniProtKB/Swiss-Prot P0AET8 (HDHA_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	bile acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	7-alpha-hydroxysteroid dehydrogenase activity Inferred from electronic annotation. Source: EC 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

25

NAD

Sites

Active site

159

1

Proton acceptor

Binding site

146

1

Substrate

Binding site

163

1

NAD

Experimental info

Mutagenesis

146

1

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

Mutagenesis

159

1

Y → F: Loss of activity. Ref.6

Mutagenesis

159

1

Y → H: Reduces activity by 87%. Ref.6

Mutagenesis

163

1

K → I: Reduces activity by 95%. Ref.6

Mutagenesis

163

1

K → R: Reduces activity by 35%. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

255

Helix Strand Turn

Details...

Helix

4 – 7

4

Beta strand

13 – 16

4

Turn

17 – 20

4

Helix

23 – 32

10

Turn

33 – 35

3

Beta strand

37 – 44

8

Helix

45 – 56

12

Turn

57 – 59

3

Beta strand

62 – 66

5

Helix

72 – 86

15

Beta strand

91 – 94

4

Helix

108 – 118

11

Helix

120 – 135

16

Beta strand

139 – 144

6

Helix

147 – 149

3

Helix

157 – 178

22

Turn

179 – 181

3

Beta strand

182 – 189

8

Helix

195 – 200

6

Helix

203 – 209

7

Helix

210 – 212

3

Helix

221 – 232

12

Helix

234 – 236

3

Beta strand

243 – 247

5

Sequences

	Sequence		Length	Mass (Da)
	P0AET8-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 66CF70E85BD67B6D	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

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. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., 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

EMBLGenBankDDBJ

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

AP_002240.1.
NP_416136.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P0AET8.

2DBase-Ecoli

P0AET8.

Genome annotation databases

GeneID

946151.

GenomeReviews

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

KEGG

ecj:JW1611.
eco:b1619.

Organism-specific databases

EchoBASE

EB0420.

EcoGene

EG10425. hdhA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AET8.

OMA

P0AET8. WRCDITS.

Enzyme and pathway databases

BioCyc

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

Family and domain databases

InterPro

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

Gene3D

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

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

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:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)