ID BA72_EUBSP STANDARD; PRT; 249 AA. AC P19337; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE 7-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) (Bile acid 7- DE dehydroxylase) (7-alpha-HSDH) (Bile acid-inducible protein). GN Name=baiA2; OS Eubacterium sp. (strain VPI 12708). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=29347; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=91072253; PubMed=2254270; RA Mallonee D.H., White W.B., Hylemon P.B.; RT "Cloning and sequencing of a bile acid-inducible operon from RT Eubacterium sp. strain VPI 12708."; RL J. Bacteriol. 172:7011-7019(1990). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=90330548; PubMed=2376563; RA Gopal-Srivastava R., Mallonee D.H., White W.B., Hylemon P.B.; RT "Multiple copies of a bile acid-inducible gene in Eubacterium sp. RT strain VPI 12708."; RL J. Bacteriol. 172:4420-4426(1990). RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=90264339; PubMed=2345152; RA Mallonee D.H., White W.B., Hylemon P.B.; RT "Nucleotide sequences and mutational analysis of the structural genes RT for nitrogenase 2 of Azotobacter vinelandii."; RL J. Bacteriol. 172:3400-3408(1990). RN [4] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=89008068; PubMed=3170477; RA White W.B., Franklund C.V., Coleman J.P., Hylemon P.B.; RT "Evidence for a multigene family involved in bile acid 7- RT dehydroxylation in Eubacterium sp. strain VPI 12708."; RL J. Bacteriol. 170:4555-4561(1988). CC -!- FUNCTION: 7-alpha-dehydroxylation of cholic acid, yielding CC deoxycholic acid and lithocholic acid, respectively. Highest CC affinity with taurochenodeoxycholic acid. CC -!- CATALYTIC ACTIVITY: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta- CC cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta- CC cholanate + NADH. CC -!- PATHWAY: Bile acid catabolism. CC -!- INDUCTION: Presence of C(24) bile acids containing a 7-alpha- CC hydroxy group. CC -!- MISCELLANEOUS: There are three genes for BAIA proteins: BAIA1 is CC identical to BAIA3 and there is 81% identity with BAIA2. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M22623; AAB61150.1; -. DR EMBL; U57489; AAC45414.1; -. DR PIR; A31841; A31841. DR HSSP; Q01782; 1E7W. DR InterPro; IPR002198; ADH_short. DR InterPro; IPR002347; Adh_short_C2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Bile acid catabolism; Multigene family; NAD; Oxidoreductase. FT NP_BIND 7 13 NAD (Potential). FT NP_BIND 32 36 NAD (Potential). FT ACT_SITE 157 157 Proton acceptor (By similarity). FT BINDING 144 144 Substrate (By similarity). SQ SEQUENCE 249 AA; 26538 MW; 9A39B78BB63DC5AF CRC64; MNLVQDKVTI ITGGTRGIGF AAAKIFIDNG AKVSIFGETQ EEVDTALAQL KELYPEEEVL GFAPDLTSRD AVMAAVGQVA QKYGRLDVMI NNAGITSNNV FSRVSEEEFK HIMDINVTGV FNGAWCAYQC MKDAKKGVII NTASVTGIFG SLSGVGYPAS KASVIGLTHG LGREIIRKNI RVVGVAPGVV NTDMTNGNPP EIMEGYLKAL PMKRMLEPEE IANVYLFLAS DLASGITATT VSVDGAYRP //