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Database: UniProt
Entry: C0CJB2_9FIRM
LinkDB: C0CJB2_9FIRM
Original site: C0CJB2_9FIRM 
ID   C0CJB2_9FIRM            Unreviewed;       393 AA.
AC   C0CJB2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   11-MAY-2016, entry version 38.
DE   RecName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE            Short=TER {ECO:0000256|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.44 {ECO:0000256|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN   ORFNames=RUMHYD_00930 {ECO:0000313|EMBL:EEG50160.1};
OS   Blautia hydrogenotrophica DSM 10507.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Blautia.
OX   NCBI_TaxID=476272 {ECO:0000313|EMBL:EEG50160.1, ECO:0000313|Proteomes:UP000003100};
RN   [1] {ECO:0000313|EMBL:EEG50160.1, ECO:0000313|Proteomes:UP000003100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10507 {ECO:0000313|EMBL:EEG50160.1,
RC   ECO:0000313|Proteomes:UP000003100};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG50160.1, ECO:0000313|Proteomes:UP000003100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10507 {ECO:0000313|EMBL:EEG50160.1,
RC   ECO:0000313|Proteomes:UP000003100};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Blautia hydrogenotrophica DSM 10507
RT   (Ruminococcus hydrogenotrophicus DSM 10507).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the fatty acid synthesis (FAS II). Catalyzes
CC       the reduction of a carbon-carbon double bond in an enoyl moiety
CC       that is covalently linked to a coenzyme A (CoA).
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + NAD(+) = trans-didehydroacyl-CoA +
CC       NADH. {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01838,
CC       ECO:0000256|SAAS:SAAS00308829}.
CC   -!- SIMILARITY: Belongs to the TER reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00537987}.
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DR   EMBL; ACBZ01000040; EEG50160.1; -; Genomic_DNA.
DR   RefSeq; WP_005946544.1; NZ_GG657679.1.
DR   STRING; 476272.RUMHYD_00930; -.
DR   EnsemblBacteria; EEG50160; EEG50160; RUMHYD_00930.
DR   PATRIC; 38359455; VBIBlaHyd72091_0736.
DR   eggNOG; ENOG4105RKW; Bacteria.
DR   eggNOG; COG3007; LUCA.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000003100; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01838; FabV_reductase; 1.
DR   InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR   InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR   InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR   Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR   Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR   Pfam; PF12241; Enoyl_reductase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000003100};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00420070};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00420073};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00420085};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00420074};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00420068};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00420088}.
FT   DOMAIN       81    311       Enoyl_reductase. {ECO:0000259|Pfam:
FT                                PF12241}.
FT   DOMAIN      318    381       Eno-Rase_FAD_bd. {ECO:0000259|Pfam:
FT                                PF07055}.
FT   NP_BIND      47     52       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND      73     74       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     110    111       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     138    139       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     268    270       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   ACT_SITE    232    232       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     241    241       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   SITE         74     74       Plays an important role in discriminating
FT                                NADH against NADPH. {ECO:0000256|HAMAP-
FT                                Rule:MF_01838}.
SQ   SEQUENCE   393 AA;  43700 MW;  D21D51EEF96039A7 CRC64;
     MIVEPKVREY ICTTAHPAGC EENVREQIAY VKAQGPKAGP KKVLVIGAST GYGLASRITA
     AFGCQAATLG IMFERPASGK RTATAGWYNT AAFEKFATQD GLYAKSINGD AFSAEVKKQA
     IDIIRRDLGQ VDLVVYSLAA PRRSADGVTY SSTLKTVGSP FTEKSIDLRT NEIVTKSVEP
     ATDKEIEGTI KVMGGEDWED WIKVLQKAGV LAENAKTVAY SYIGPELTYP IYTHGTIGQA
     KNHLQKTAEK MNQELNGVTA VVSVNKALVT QASSAIPIVP LYLSILYKIM KEQGSHEDCI
     RQMDRLFRTK LLENPMPVDQ EGRIRMDDWE LDEKVQAEVM KVWAMMSTEN LKEVSDIDGY
     WEDFYKMFGF RFEQVDYSQD VDVDVRIPSL EEN
//
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