ID   FABV_SHEB9              Reviewed;         400 AA.
AC   A9KWI3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000255|HAMAP-Rule:MF_01838};
DE            Short=ENR {ECO:0000255|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000255|HAMAP-Rule:MF_01838};
GN   OrderedLocusNames=Sbal195_1633;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC       fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-
CC       carbon double bond in an enoyl moiety that is covalently linked to an
CC       acyl carrier protein (ACP). {ECO:0000255|HAMAP-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, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01838};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01838}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC   -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01838}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000891; ABX48806.1; -; Genomic_DNA.
DR   RefSeq; WP_006085369.1; NC_009997.1.
DR   AlphaFoldDB; A9KWI3; -.
DR   SMR; A9KWI3; -.
DR   EnsemblBacteria; ABX48806; ABX48806; Sbal195_1633.
DR   GeneID; 11771867; -.
DR   KEGG; sbn:Sbal195_1633; -.
DR   HOGENOM; CLU_057698_1_0_6; -.
DR   OMA; EGCIEQI; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000770; 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;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..400
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT                   /id="PRO_1000088456"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         48..53
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         74..75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         111..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         139..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         273..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   SITE            75
FT                   /note="Plays an important role in discriminating NADH
FT                   against NADPH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
SQ   SEQUENCE   400 AA;  44058 MW;  26F8CCF620513976 CRC64;
     MIIKPKIRGF ICTTTHPVGC EANVQEQITL TKAKGKIANG PKRVLVVGSS SGYGLSSRIA
     AAFGSDAATI GVFFEKPGTE TKPGTAGWYN SAAFDKFAKA EGLYSKSINC DAFSHEAKQK
     VIELIKQDLG EIDMVVYSLA SPVRKLPDSG ELIRSALKPI GETYTATAVD TNKDCIIEAT
     VEPATEQEIA DTVTVMGGED WELWIKALSE AGVLADNCKT VAYSYIGTEL TWPIYWHGAL
     GKAKMDLDRA AKALNEQLSA TGGSANVAVL KSVVTQASSA IPVMPLYIAM VFKKMRQEGL
     HEGCMEQIYR MFSERLFRAD GAKPETDSDN RIRLDDWELR EDIQQHCRNL WPQVTTENLS
     ELTDYREYKA EFIKLFGFGI EGIDYDADVN PYVEFDVIEL