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   27-MAR-2024, entry version 161.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI;
DE            Short=ENR;
DE            EC=1.3.1.9;
DE   AltName: Full=Cold shock-induced protein 15;
DE            Short=CSI15;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
DE   AltName: Full=Vegetative protein 241;
DE            Short=VEG241;
GN   Name=fabI; Synonyms=yjbW; OrderedLocusNames=BSU11720;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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, AND INDUCTION.
RC   STRAIN=168 / JH642;
RX   PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
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   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   FUNCTION AS AN ENOYL-ACP REDUCTASE AND IN FATTY ACID BIOSYNTHESIS,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY 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 Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 275:40128-40133(2000).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR,
RP   ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=21185310; DOI=10.1016/j.jmb.2010.12.003;
RA   Kim K.H., Ha B.H., Kim S.J., Hong S.K., Hwang K.Y., Kim E.E.;
RT   "Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B.
RT   subtilis.";
RL   J. Mol. Biol. 406:403-415(2011).
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. {ECO:0000269|PubMed:11007778}.
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         Evidence={ECO:0000269|PubMed:11007778};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10242;
CC         Evidence={ECO:0000269|PubMed:11007778};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-[ACP] + H(+) + NADH = butanoyl-[ACP] + NAD(+);
CC         Xref=Rhea:RHEA:54868, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC         Evidence={ECO:0000269|PubMed:11007778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54869;
CC         Evidence={ECO:0000269|PubMed:11007778};
CC   -!- ACTIVITY REGULATION: Inhibited by triclosan and acrylamide.
CC       {ECO:0000269|PubMed:11007778, ECO:0000269|PubMed:21185310}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7 uM for NADH {ECO:0000269|PubMed:11007778};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21185310}.
CC   -!- INDUCTION: By cold shock. {ECO:0000269|PubMed:8755892}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FabI subfamily. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13029.2; -; Genomic_DNA.
DR   PIR; G69845; G69845.
DR   RefSeq; NP_389054.2; NC_000964.3.
DR   RefSeq; WP_003232896.1; NZ_JNCM01000035.1.
DR   PDB; 3OIF; X-ray; 2.60 A; A/B/C/D=1-258.
DR   PDB; 3OIG; X-ray; 1.25 A; A=1-258.
DR   PDBsum; 3OIF; -.
DR   PDBsum; 3OIG; -.
DR   AlphaFoldDB; P54616; -.
DR   SMR; P54616; -.
DR   IntAct; P54616; 1.
DR   MINT; P54616; -.
DR   STRING; 224308.BSU11720; -.
DR   BindingDB; P54616; -.
DR   ChEMBL; CHEMBL1075044; -.
DR   DrugCentral; P54616; -.
DR   SwissLipids; SLP:000001776; -.
DR   jPOST; P54616; -.
DR   PaxDb; 224308-BSU11720; -.
DR   EnsemblBacteria; CAB13029; CAB13029; BSU_11720.
DR   GeneID; 83884462; -.
DR   GeneID; 939379; -.
DR   KEGG; bsu:BSU11720; -.
DR   PATRIC; fig|224308.179.peg.1261; -.
DR   eggNOG; COG0623; Bacteria.
DR   InParanoid; P54616; -.
DR   OrthoDB; 9803628at2; -.
DR   PhylomeDB; P54616; -.
DR   BioCyc; BSUB:BSU11720-MONOMER; -.
DR   BioCyc; MetaCyc:BSU11720-MONOMER; -.
DR   BRENDA; 1.3.1.9; 658.
DR   SABIO-RK; P54616; -.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; P54616; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR   GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR   GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR   CDD; cd05372; ENR_SDR; 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   InterPro; IPR002347; SDR_fam.
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   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NAD; NADP;
KW   Oxidoreductase; Reference proteome; Stress response.
FT   CHAIN           1..258
FT                   /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT                   /id="PRO_0000054895"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT   BINDING         14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:21185310"
FT   BINDING         20..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:21185310"
FT   BINDING         67..68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:21185310"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:21185310"
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:0000269|PubMed:21185310"
FT   BINDING         194..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:21185310"
FT   SITE            206
FT                   /note="Involved in acyl-ACP binding"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        20
FT                   /note="S -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..13
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           21..31
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           46..54
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           72..85
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           124..133
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           159..179
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          184..191
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:3OIF"
FT   HELIX           205..215
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           224..235
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:3OIG"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:3OIG"
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
//