(data stored in ACNUC7421 zone)

SWISSPROT: A0KEB7_AERHH

ID   A0KEB7_AERHH            Unreviewed;       395 AA.
AC   A0KEB7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   13-FEB-2019, entry version 78.
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   OrderedLocusNames=AHA_0052 {ECO:0000313|EMBL:ABK37443.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37443.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37443.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP]
CC         + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925,
CC         Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785;
CC         EC=1.3.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01838};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01838,
CC       ECO:0000256|SAAS:SAAS00946236}.
CC   -!- SIMILARITY: Belongs to the TER reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946247}.
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DR   EMBL; CP000462; ABK37443.1; -; Genomic_DNA.
DR   RefSeq; WP_011704090.1; NC_008570.1.
DR   RefSeq; YP_854577.1; NC_008570.1.
DR   STRING; 380703.AHA_0052; -.
DR   EnsemblBacteria; ABK37443; ABK37443; AHA_0052.
DR   GeneID; 4490272; -.
DR   KEGG; aha:AHA_0052; -.
DR   PATRIC; fig|380703.7.peg.47; -.
DR   eggNOG; ENOG4105RKW; Bacteria.
DR   eggNOG; COG3007; LUCA.
DR   HOGENOM; HOG000269390; -.
DR   KO; K00209; -.
DR   OMA; EDWESWI; -.
DR   BioCyc; AHYD380703:G1G7B-52-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR37480; PTHR37480; 1.
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;
DR   PRODOM; A0KEB7.
DR   SWISS-2DPAGE; A0KEB7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00946244};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00946248};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00946246};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00946258};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946240};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00946243, ECO:0000313|EMBL:ABK37443.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN       82    315       Enoyl_reductase. {ECO:0000259|Pfam:
FT                                PF12241}.
FT   DOMAIN      323    385       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     271    273       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   ACT_SITE    233    233       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     242    242       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   395 AA;  42545 MW;  0E1E49AB7150F7C6 CRC64;
     MIIHPQIQGC VARNCHPIGC RAAVLQQIAS VRAAGSFNGP KRVLVLGASS GFGLASRIAL
     TFGAGADTVG VSFERGPSDK GPGSAGWYNN IWFRKEAEQT GRIAINLIGD AFSIGMRQQA
     IDTIRQQLGQ VDLVIYSLAS GIRVLPDGTQ VRSVLKTTSQ PFSGWGLDLE HDTLVQQSLD
     PATPEEIRDT VSVMGGEDWQ LWLQALQQAD CLAPGAQTVA YSYIGPESTY PLYRDGTIGY
     AKEHLHATAE TINLQLAELG GHAWVSVCKA LVTKASAYIP VLPVYLGLLM GVMKERGVHE
     GCIEQMQRLF ATKMYGPQGV VADGNRLIRM DDHELDPAIQ AAVSALWSKV TPDNFHALGD
     FAGLRQDFMQ LNGFELPGVD YGAPVDLASL TELLP
//

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