ID   FABI_RICFE              Reviewed;         260 AA.
AC   Q4ULZ7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI;
DE            Short=ENR;
DE            EC=1.3.1.9;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
GN   Name=fabI; OrderedLocusNames=RF_0575;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an
CC       enoyl moiety that is covalently linked to an acyl carrier protein
CC       (ACP). Involved in the elongation cycle of fatty acid which are used in
CC       the lipid metabolism (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FabI subfamily. {ECO:0000305}.
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DR   EMBL; CP000053; AAY61426.1; -; Genomic_DNA.
DR   RefSeq; WP_011270907.1; NC_007109.1.
DR   AlphaFoldDB; Q4ULZ7; -.
DR   SMR; Q4ULZ7; -.
DR   STRING; 315456.RF_0575; -.
DR   EnsemblBacteria; AAY61426; AAY61426; RF_0575.
DR   KEGG; rfe:RF_0575; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_5; -.
DR   OMA; GILDMIH; -.
DR   OrthoDB; 762291at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR   CDD; cd05372; ENR_SDR; 1.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43159; PTHR43159; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..260
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000286636"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         21..22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  28254 MW;  14E5338B63ABDD2C CRC64;
     MTTGLLQGKK GLITGIANNM SISWAIAQLA KKHGAELWFT YQSEVLEKRV KPLAEEIGCN
     FVSELDVTNP KSISNLFDDI KEKWGSFDFL LHGMAFADKN ELKGRYVDTS LENFHNSLHI
     SCYSLLELSR SAEALMHDGG SIVTLTYYGA EKVIPNYNVM GISKAALEAS VKYLATDLGE
     NNIRVNAISA GPIKTLASSA IGDFSTMLKS HAATAPLKRN TTQEDVGGAA VYLFSNLSKG
     VTGEIHYVDC GYNIMGSNKL