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BAIN_CLOS5
ID   BAIN_CLOS5              Reviewed;         409 AA.
AC   B0NAQ4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=3-dehydro-bile acid delta(4,6)-reductase {ECO:0000303|PubMed:29217478};
DE            EC=1.3.1.114 {ECO:0000269|PubMed:29217478};
GN   Name=baiN {ECO:0000303|PubMed:29217478};
GN   ORFNames=CLOSCI_00523 {ECO:0000312|EMBL:EDS08212.1};
OS   Clostridium scindens (strain ATCC 35704 / DSM 5676 / VPI 13733 / 19).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=411468;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35704 / DSM 5676 / VPI 13733 / 19 {ECO:0000312|EMBL:EDS08212.1,
RC   ECO:0000312|Proteomes:UP000003459};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium scindens(ATCC 35704).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35704 / DSM 5676 / VPI 13733 / 19 {ECO:0000312|EMBL:EDS08212.1,
RC   ECO:0000312|Proteomes:UP000003459};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC   STRAIN=ATCC 35704 / DSM 5676 / VPI 13733 / 19;
RX   PubMed=29217478; DOI=10.1016/j.bbalip.2017.12.001;
RA   Harris S.C., Devendran S., Alves J.M.P., Mythen S.M., Hylemon P.B.,
RA   Ridlon J.M.;
RT   "Identification of a gene encoding a flavoprotein involved in bile acid
RT   metabolism by the human gut bacterium Clostridium scindens ATCC 35704.";
RL   Biochim. Biophys. Acta 1863:276-283(2018).
CC   -!- FUNCTION: Involved in the secondary bile acid metabolism. Catalyzes two
CC       subsequent reductions of the double bonds within the bile acid A/B
CC       rings of 3-oxochol-4,6-dien-24-oyl-CoA and 12alpha-hydroxy-3-oxochol-
CC       4,6-dien-24-oyl-CoA to yield 3-oxocholan-24-oyl-CoA and 12alpha-
CC       hydroxy-3-oxocholan-24-oyl-CoA, respectively.
CC       {ECO:0000269|PubMed:29217478}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxocholan-24-oyl-CoA + NAD(+) = 3-oxochol-4-en-24-oyl-CoA +
CC         H(+) + NADH; Xref=Rhea:RHEA:31735, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:86412,
CC         ChEBI:CHEBI:136703; EC=1.3.1.114;
CC         Evidence={ECO:0000269|PubMed:29217478};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxochol-4-en-24-oyl-CoA + NAD(+) = 3-oxochol-4,6-dien-24-
CC         oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:56648, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:86412,
CC         ChEBI:CHEBI:140634; EC=1.3.1.114;
CC         Evidence={ECO:0000269|PubMed:29217478};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12alpha-hydroxy-3-oxocholan-24-oyl-CoA + NAD(+) = 12alpha-
CC         hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:56652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:136701, ChEBI:CHEBI:140635;
CC         EC=1.3.1.114; Evidence={ECO:0000269|PubMed:29217478};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12alpha-hydroxy-3-oxochol-4-en-24-oyl-CoA + NAD(+) = 12alpha-
CC         hydroxy-3-oxochola-4,6-dien-24-oyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:56656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132978, ChEBI:CHEBI:140635;
CC         EC=1.3.1.114; Evidence={ECO:0000269|PubMed:29217478};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000305|PubMed:29217478};
CC   -!- PATHWAY: Lipid metabolism; bile acid degradation.
CC       {ECO:0000305|PubMed:29217478}.
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DR   EMBL; ABFY02000009; EDS08212.1; -; Genomic_DNA.
DR   RefSeq; WP_004606074.1; NZ_DS499697.1.
DR   AlphaFoldDB; B0NAQ4; -.
DR   SMR; B0NAQ4; -.
DR   STRING; 411468.CLOSCI_00523; -.
DR   EnsemblBacteria; EDS08212; EDS08212; CLOSCI_00523.
DR   GeneID; 62697204; -.
DR   KEGG; ag:EDS08212; -.
DR   eggNOG; COG2081; Bacteria.
DR   HOGENOM; CLU_025174_3_1_9; -.
DR   OrthoDB; 1513550at2; -.
DR   BioCyc; MetaCyc:BAIDEL6EUBSP-MON; -.
DR   BRENDA; 1.3.1.114; 1513.
DR   UniPathway; UPA00279; -.
DR   Proteomes; UP000003459; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0030573; P:bile acid catabolic process; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.260; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR004792; BaiN-like.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023166; HI0933-like_dom_sf.
DR   PANTHER; PTHR42887; PTHR42887; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00275; TIGR00275; 1.
PE   1: Evidence at protein level;
KW   Bile acid catabolism; FAD; Flavoprotein; Lipid degradation;
KW   Lipid metabolism; NAD; Oxidoreductase; Steroid metabolism.
FT   CHAIN           1..409
FT                   /note="3-dehydro-bile acid delta(4,6)-reductase"
FT                   /id="PRO_0000445588"
SQ   SEQUENCE   409 AA;  44417 MW;  8C748517E0F51536 CRC64;
     MNRIGIIGGG ASGIVAAIAA ARSDGDAQVF ILEQKENIGK KILATGNGRC NLTNEAMDAS
     CYHGEDPEFA RNVLKQFGYG ETLEFFASLG LFTKSRGGYI YPRSDQAASV LELLEMELRR
     QKVKIYTGVR VEALKLSAKG FVIRADGQRF PADRVILACG GKASKSLGSD GSGYALARSM
     GHTLSPVVPA LVQLKVKKHP FAKAAGVRTD AKVAALLGRQ VLAEDTGEMQ ITAYGISGIP
     VFQISRHIAK GLYEGKEMKV RVDFLPEMEA SQVRKAFNTH LDKCPYATCQ EFLTGIFPKK
     LIPRLLELSH IRQNFPASEL KPAQWEDLIR ACKQTLLTIE DTNGFDNAQV CAGGVRTGEV
     YPDTLESRYA DGLYLTGELL DVEGICGGYN LQWAWATGYL AGRAAAERP
 
 
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