ID   FABI_SHIFL              Reviewed;         262 AA.
AC   P0AEK6; P29132;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE            EC=1.3.1.9;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
GN   Name=fabI; OrderedLocusNames=SF1293, S1375;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD(+) = trans-
CC       2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- MISCELLANEOUS: The antibiotic diazaborine interferes with the
CC       activity by binding to the protein (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. FabI subfamily.
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DR   EMBL; AE005674; AAN42904.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16787.1; -; Genomic_DNA.
DR   RefSeq; NP_707197.1; -.
DR   RefSeq; NP_836980.1; -.
DR   SMR; P0AEK6; 2-260.
DR   GeneID; 1024254; -.
DR   GeneID; 1077753; -.
DR   GenomeReviews; AE005674_GR; SF1293.
DR   GenomeReviews; AE014073_GR; S1375.
DR   KEGG; sfl:SF1293; -.
DR   KEGG; sfx:S1375; -.
DR   HOGENOM; P0AEK6; -.
DR   OMA; P0AEK6; ECDVGSD.
DR   BioCyc; SFLE198214:AAN42904.1-MON; -.
DR   BRENDA; 1.3.1.9; 189495.
DR   BindingDB; P0AEK6; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NAD...; IEA:EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   PANTHER; PTHR19410:SF12; Enoyl-ACP_rdct; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane;
KW   Complete proteome; Fatty acid biosynthesis; Lipid synthesis; Membrane;
KW   NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    262       Enoyl-[acyl-carrier-protein] reductase
FT                                [NADH].
FT                                /FTId=PRO_0000054911.
FT   NP_BIND      10     36       NAD (By similarity).
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
SQ   SEQUENCE   262 AA;  27864 MW;  436A89AF349D1866 CRC64;
     MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV
     LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS
     SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE
     GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI
     SGEVVHVDGG FSIAAMNELE LK
//