ID   FABI_BUCAP              Reviewed;         260 AA.
AC   Q8K9Q6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=BUsg_255;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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 and in the biotin biosynthesis (By similarity).
CC       {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   -!- PATHWAY: Cofactor biosynthesis; biotin 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; AE013218; AAM67813.1; -; Genomic_DNA.
DR   RefSeq; WP_011053780.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9Q6; -.
DR   SMR; Q8K9Q6; -.
DR   STRING; 198804.BUsg_255; -.
DR   EnsemblBacteria; AAM67813; AAM67813; BUsg_255.
DR   KEGG; bas:BUsg_255; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_6; -.
DR   OMA; GILDMIH; -.
DR   OrthoDB; 762291at2; -.
DR   UniPathway; UPA00078; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000416; 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:0009102; P:biotin biosynthetic process; 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   PANTHER; PTHR43159; PTHR43159; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase.
FT   CHAIN           1..260
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000054897"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         192..196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            201
FT                   /note="Involved in acyl-ACP binding"
FT                   /evidence="ECO:0000250"
FT   SITE            204
FT                   /note="Involved in acyl-ACP binding"
FT                   /evidence="ECO:0000250"
FT   SITE            205
FT                   /note="Involved in acyl-ACP binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  29268 MW;  B97D1279FEFD3C71 CRC64;
     MGILKGKKIL ITGILNEKSI AFGIAKSMYK QEAELIFVCQ NKKIINKIKY LIKSINYNTI
     FFCDVSHDEN IKELFFNIKK VWNNFDGLVH SIAYCPKKQM HEDFVESSSR KSFNICHEIS
     SYSFLSMARE CKNMLNKFSS LVTLSYLGSQ KIVSNYNMMG LAKSSLEANV RYMANSLGKN
     NIRVNAISSG PIKTTSSYQI KNFNKIQKIH KLFSLTKNHV SSEEIGNVAA FLCSDLSIGI
     TGSIINVDHG FNLNGINSII