ID   FABV_COXBU              Reviewed;         406 AA.
AC   Q83EP5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=CBU_0270;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
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DR   EMBL; AE016828; AAO89828.1; -; Genomic_DNA.
DR   RefSeq; NP_819314.1; NC_002971.3.
DR   RefSeq; WP_010957471.1; NC_002971.4.
DR   AlphaFoldDB; Q83EP5; -.
DR   SMR; Q83EP5; -.
DR   STRING; 227377.CBU_0270; -.
DR   EnsemblBacteria; AAO89828; AAO89828; CBU_0270.
DR   GeneID; 1208151; -.
DR   KEGG; cbu:CBU_0270; -.
DR   PATRIC; fig|227377.7.peg.264; -.
DR   eggNOG; COG3007; Bacteria.
DR   HOGENOM; CLU_057698_1_0_6; -.
DR   OrthoDB; 9802260at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR   GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 1.
DR   PANTHER; PTHR37480:SF1; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]; 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; Reference proteome.
FT   CHAIN           1..406
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT                   /id="PRO_0000220042"
FT   ACT_SITE        236
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         140..141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT   BINDING         275..277
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   406 AA;  44875 MW;  15AFFE9E75FDCF32 CRC64;
     MIVQPKVRGF ICTTAHPEGC ARHVGEWINY AKQEPSLTGG PQKVLIIGAS TGFGLASRIV
     AAFGAGAKTI GVFFERPASG KRTASPGWYN TAAFEKTALA AGLYAKSING DAFSDEIKQQ
     TIDLIQKDWQ GGVDLVIYSI ASPRRVHPRT GEIFNSVLKP IGQTYHNKTV DVMTGEVSPV
     SIEPATEKEI RDTEAVMGGD DWALWINALF KYNCLAEGVK TVAFTYIGPE LTHAVYRNGT
     IGRAKLHLEK TARELDTQLE SALSGQALIS VNKALVTQAS AAIPVVPLYI SLLYKIMKEK
     NIHEGCIEQM WRLFKERLYS NQNIPTDSEG RIRIDDWEMR EDVQAEIKRL WESINTGNVE
     TVSDIAGYRE DFYKLFGFGL NGIDYERGVE IEKAIPSITV TPENPE
//