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Database: UniProt
Entry: Q1Z450_PHOPR
LinkDB: Q1Z450_PHOPR
Original site: Q1Z450_PHOPR 
ID   Q1Z450_PHOPR            Unreviewed;       400 AA.
AC   Q1Z450;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   20-JAN-2016, entry version 38.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE            Short=ENR {ECO:0000256|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.9 {ECO:0000256|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN   ORFNames=P3TCK_27639 {ECO:0000313|EMBL:EAS43252.1};
OS   Photobacterium profundum 3TCK.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS43252.1, ECO:0000313|Proteomes:UP000003789};
RN   [1] {ECO:0000313|EMBL:EAS43252.1, ECO:0000313|Proteomes:UP000003789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3TCK {ECO:0000313|EMBL:EAS43252.1,
RC   ECO:0000313|Proteomes:UP000003789};
RA   Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA   Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J.,
RA   Kravitz S., Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the final reduction of the elongation cycle
CC       of fatty acid synthesis (FAS II). Catalyzes the reduction of a
CC       carbon-carbon double bond in an enoyl moiety that is covalently
CC       linked to an acyl carrier protein (ACP). {ECO:0000256|HAMAP-
CC       Rule:MF_01838}.
CC   -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
CC       trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
CC       {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:SAAS00341357}.
CC   -!- SIMILARITY: Belongs to the TER reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAS43252.1}.
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DR   EMBL; AAPH01000012; EAS43252.1; -; Genomic_DNA.
DR   RefSeq; WP_006233094.1; NZ_CH724136.1.
DR   EnsemblBacteria; EAS43252; EAS43252; P3TCK_27639.
DR   PATRIC; 30921305; VBIPhoPro77067_4207.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000003789; Unassembled WGS sequence.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; 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; IPR016040; NAD(P)-bd_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.
DR   SUPFAM; SSF51735; SSF51735; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000003789};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308828};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308833};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308838};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308827};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00308822};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00008249}.
FT   DOMAIN       84    319       Enoyl_reductase. {ECO:0000259|Pfam:
FT                                PF12241}.
FT   DOMAIN      327    390       Eno-Rase_FAD_bd. {ECO:0000259|Pfam:
FT                                PF07055}.
FT   NP_BIND      48     53       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND      75     76       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     112    113       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     141    142       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     275    277       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   ACT_SITE    237    237       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     227    227       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     246    246       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   SITE         76     76       Plays an important role in discriminating
FT                                NADH against NADPH. {ECO:0000256|HAMAP-
FT                                Rule:MF_01838}.
SQ   SEQUENCE   400 AA;  43883 MW;  1E9C2B64F2F0EFB0 CRC64;
     MIIEPVVKGV VARSAHPFGC QQAIRNQINY VRTADPVTDG PKKVLVLGAS SGFGLASRIS
     LAFGGSMADT IGISFERGPS EKGVGTAGWY NNIFFREEAE KAGLIGKNFI GDAFSPQMRQ
     QVIEYIKTEF GGQLDLVVYS LATGVRPNPE TGELWRSSIK TMGEPVTGPT INIETDTMEQ
     MTIGTATPEE VEDTEKVMGG EDWASWIDIL SDAGVLATGC KTVAYSYVGP KATYPIYHQG
     TLGRAKAHLH ATADQLNNKM SEMGGEAYVS VCKALVTKAS VFIPAFSPYI LALFKVMKDK
     GVHEGCIEQM QRLYAQRLYG KDKIVPVDDN RLIRVDDWEL EDDIQQQVSE LMAKITPENF
     TTMGDYQGYK TDFMQLNGFD LEGVDYQADI SFETLTQLVA
//
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