ID   FABI_BUCAI              Reviewed;         260 AA.
AC   P57353;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=BU265;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB12975.1; -; Genomic_DNA.
DR   RefSeq; NP_240089.1; NC_002528.1.
DR   RefSeq; WP_010896033.1; NC_002528.1.
DR   AlphaFoldDB; P57353; -.
DR   SMR; P57353; -.
DR   STRING; 563178.BUAP5A_260; -.
DR   EnsemblBacteria; BAB12975; BAB12975; BAB12975.
DR   KEGG; buc:BU265; -.
DR   PATRIC; fig|107806.10.peg.275; -.
DR   eggNOG; COG0623; Bacteria.
DR   HOGENOM; CLU_010194_10_1_6; -.
DR   UniPathway; UPA00078; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
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   Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR   PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000054896"
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            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;  28779 MW;  DCA04AC740D6DADD CRC64;
     MGFLKGKKFL IIGISSVRSI AFGIAKSLYN QKAELGFVCQ NEKIRKKIKK LVEPMKSCIV
     LCCDVSNDKN IKKLFIDLGQ VWKKFDGLVH AIAYCPKQYF NGDFIDNITR EGFNISHEIS
     SYSFIGLVKA CRTMLNNFSS LLTLSYLGSQ RVVPNYNVMG LAKASLEASV RYMASSLGKE
     NIRVNAISSS PIKTISSYKI TNFNKIRNCS YASSFLKNSV TSENIGNVAS FLLSDLSLGI
     TGSVIYVDNG FNVSSMNNIQ
//