ID   FABI_BACSU              Reviewed;         258 AA.
AC   P54616; O31621;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE            EC=1.3.1.9;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
DE   AltName: Full=Cold shock-induced protein 15;
DE            Short=CSI15;
DE   AltName: Full=Vegetative protein 241;
DE            Short=VEG241;
GN   Name=fabI; Synonyms=yjbW; OrderedLocusNames=BSU11720;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-21.
RC   STRAIN=168 / JH642;
RX   MEDLINE=96345629; PubMed=8755892;
RA   Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT   "Cold shock stress-induced proteins in Bacillus subtilis.";
RL   J. Bacteriol. 178:4611-4619(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=168 / IS58;
RX   MEDLINE=97443988; PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [4]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
RP   REGULATION.
RX   PubMed=11007778; DOI=10.1074/jbc.M005611200;
RA   Heath R.J., Su N., Murphy C.K., Rock C.O.;
RT   "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from
RT   Bacillus subtilis.";
RL   J. Biol. Chem. 275:40128-40133(2000).
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD(+) = trans-
CC       2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
CC   -!- ENZYME REGULATION: Inhibited by triclosan.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7 uM for NADH;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- INDUCTION: By cold shock.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. FabI subfamily.
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DR   EMBL; AL009126; CAB13029.2; -; Genomic_DNA.
DR   PIR; G69845; G69845.
DR   RefSeq; NP_389054.2; -.
DR   HSSP; P29132; 1DFI.
DR   GeneID; 939379; -.
DR   GenomeReviews; AL009126_GR; BSU11720.
DR   KEGG; bsu:BSU11720; -.
DR   NMPDR; fig|224308.1.peg.1173; -.
DR   SubtiList; BG13152; fabI.
DR   HOGENOM; P54616; -.
DR   OMA; P54616; LVHCLAF.
DR   BioCyc; BSUB224308:BSU1173-MON; -.
DR   BRENDA; 1.3.1.9; 150.
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:0006950; P:response to stress; 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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Fatty acid biosynthesis;
KW   Lipid synthesis; NAD; Oxidoreductase; Stress response.
FT   CHAIN         1    258       Enoyl-[acyl-carrier-protein] reductase
FT                                [NADH].
FT                                /FTId=PRO_0000054895.
FT   NP_BIND      11     37       NAD (By similarity).
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   CONFLICT     20     20       S -> Q (in Ref. 2; AA sequence).
SQ   SEQUENCE   258 AA;  27874 MW;  097667168B3F0470 CRC64;
     MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH ELAGTLDRND
     SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK EELVGEYLNT NRDGFLLAHN
     ISSYSLTAVV KAARPMMTEG GSIVTLTYLG GELVMPNYNV MGVAKASLDA SVKYLAADLG
     KENIRVNSIS AGPIRTLSAK GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR
     GITGENLHVD SGFHITAR
//