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Reviewed, UniProtKB/Swiss-Prot P0AET8 (HDHA_ECOLI)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2552557-alpha-hydroxysteroid dehydrogenase
PRO_0000054708

Regions

Nucleotide binding18 – 4225NAD

Sites

Active site1591Proton acceptor
Binding site1461Substrate
Binding site1631NAD

Experimental info

Mutagenesis1461S → A or H: Reduces activity by over 65%. Ref.6
Mutagenesis1591Y → F: Loss of activity. Ref.6
Mutagenesis1591Y → H: Reduces activity by 87%. Ref.6
Mutagenesis1631K → I: Reduces activity by 95%. Ref.6
Mutagenesis1631K → R: Reduces activity by 35%. Ref.6

Secondary structure

.......................................... 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AET8-1 [UniParc].

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

FASTA25526,779
        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' 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. expand/collapse author list , 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

D10497 Genomic DNA. Translation: BAA01384.1.
U00096 Genomic DNA. Translation: AAC74691.1.
AP009048 Genomic DNA. Translation: BAA15370.1.
M14641 Genomic DNA. Translation: AAA68921.1.
PIRA38527.
RefSeqAP_002240.1.
NP_416136.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AHHX-ray2.30A/B1-255[»]
1AHIX-ray2.30A/B1-255[»]
1FMCX-ray1.80A/B1-255[»]
ModBaseSearch...

2-D gel databases

SWISS-2DPAGEP0AET8.
2DBase-EcoliP0AET8.

Genome annotation databases

GeneID946151.
GenomeReviewsGene locus JW1611 in contig AP009048_GR.
Gene locus b1619 in contig U00096_GR.
KEGGecj:JW1611.
eco:b1619.

Organism-specific databases

EchoBASEEB0420.
EcoGeneEG10425. hdhA.
CMRSearch...

Phylogenomic databases

HOGENOMP0AET8.
OMAP0AET8. WRCDITS.

Enzyme and pathway databases

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

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDHA_ECOLI
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents