ID   FABI_NOSS1              Reviewed;         258 AA.
AC   Q05069;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 124.
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=all4391;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8391534; DOI=10.1128/jb.175.13.4025-4035.1993;
RA   Wei T.-F., Ramasubramanian T.S., Pu F., Golden J.W.;
RT   "Anabaena sp. strain PCC 7120 bifA gene encoding a sequence-specific DNA-
RT   binding protein cloned by in vivo transcriptional interference selection.";
RL   J. Bacteriol. 175:4025-4035(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD04184.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB76090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L10036; AAD04184.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000019; BAB76090.1; ALT_INIT; Genomic_DNA.
DR   PIR; AG2354; AG2354.
DR   RefSeq; WP_041456288.1; NZ_RSCN01000051.1.
DR   AlphaFoldDB; Q05069; -.
DR   SMR; Q05069; -.
DR   STRING; 103690.17133527; -.
DR   EnsemblBacteria; BAB76090; BAB76090; BAB76090.
DR   GeneID; 58726068; -.
DR   KEGG; ana:all4391; -.
DR   eggNOG; COG0623; Bacteria.
DR   OMA; GILDMIH; -.
DR   OrthoDB; 762291at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002483; 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; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000054893"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        158
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         67..68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   258 AA;  27421 MW;  45012CA8497E001B CRC64;
     MLNLTGKNAL VTGIANNRSI AWGIAQQLHA AGANLGITYL PDERGKFEKK VSELVEPLNP
     SLFLPCNVQN DEQIQSTFDT IRDKWGRLDI LIHCLAFANR DDLTGDFSQT SRAGFATALD
     ISTFSLVQLS GAAKPLMTEG GSIITLSYLG GVRAVPNYNV MGVAKAGLEA SVRYLASELG
     SQNIRVNAIS AGPIRTLASS AVGGILDMIH HVEQVAPLRR TVTQLEVGNT AAFLASDLAS
     GITGQVLYVD AGYEIMGM