HDHA_ECO57
ID HDHA_ECO57 Reviewed; 255 AA.
AC P0AET9; P25529;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=7alpha-hydroxysteroid dehydrogenase {ECO:0000250|UniProtKB:P0AET8};
DE Short=7alpha-HSDH {ECO:0000250|UniProtKB:P0AET8};
DE EC=1.1.1.159 {ECO:0000250|UniProtKB:P0AET8};
DE AltName: Full=NAD-dependent 7alpha-hydroxysteroid dehydrogenase {ECO:0000250|UniProtKB:P0AET8};
GN Name=hdhA; OrderedLocusNames=Z2624, ECs2327;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: 7alpha-hydroxysteroid dehydrogenase involved in the
CC metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of
CC the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major
CC human bile acids cholate and chenodeoxycholate, to the corresponding 7-
CC oxosteroids. To a lesser extent, can also act on
CC taurochenodeoxycholate, taurocholate and glycocholate. Can also use
CC glycochenodeoxycholate as substrate. Is not able to use NADP(+) instead
CC of NAD(+) as the electron acceptor. {ECO:0000250|UniProtKB:P0AET8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-
CC cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.159;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH;
CC Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + taurochenodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADH; Xref=Rhea:RHEA:53824, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53825;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + taurocholate = 7-oxo-taurodeoxycholate + H(+) + NADH;
CC Xref=Rhea:RHEA:53848, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137820;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53849;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycocholate + NAD(+) = 7-oxo-glycodeoxycholate + H(+) + NADH;
CC Xref=Rhea:RHEA:53852, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137824;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53853;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate + NAD(+) = 7-oxoglycolithocholate +
CC H(+) + NADH; Xref=Rhea:RHEA:53844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000250|UniProtKB:P0AET8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53845;
CC Evidence={ECO:0000250|UniProtKB:P0AET8};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AET8}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000250|UniProtKB:P0AET8}.
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DR EMBL; AE005174; AAG56608.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35750.1; -; Genomic_DNA.
DR PIR; D85768; D85768.
DR PIR; G90919; G90919.
DR RefSeq; NP_310354.1; NC_002695.1.
DR RefSeq; WP_000483353.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P0AET9; -.
DR SMR; P0AET9; -.
DR STRING; 155864.EDL933_2573; -.
DR EnsemblBacteria; AAG56608; AAG56608; Z2624.
DR EnsemblBacteria; BAB35750; BAB35750; ECs_2327.
DR GeneID; 912528; -.
DR KEGG; ece:Z2624; -.
DR KEGG; ecs:ECs_2327; -.
DR PATRIC; fig|386585.9.peg.2437; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; VYLCCKA; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0106281; F:chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Bile acid catabolism; Lipid degradation; Lipid metabolism; NAD;
KW Oxidoreductase; Reference proteome; Steroid metabolism.
FT CHAIN 1..255
FT /note="7alpha-hydroxysteroid dehydrogenase"
FT /id="PRO_0000054709"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 42..43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 68..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 99
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 146
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 151
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 159
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT SITE 146
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
FT SITE 163
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P0AET8"
SQ SEQUENCE 255 AA; 26779 MW; 66CF70E85BD67B6D CRC64;
MFNSDNLRLD GKCAIITGAG AGIGKEIAIT FATAGASVVV SDINADAANH VVDEIQQLGG
QAFACRCDIT SEQELSALAD FAISKLGKVD ILVNNAGGGG PKPFDMPMAD FRRAYELNVF
SFFHLSQLVA PEMEKNGGGV ILTITSMAAE NKNINMTSYA SSKAAASHLV RNMAFDLGEK
NIRVNGIAPG AILTDALKSV ITPEIEQKML QHTPIRRLGQ PQDIANAALF LCSPAASWVS
GQILTVSGGG VQELN
