FABI_BACSU
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 03-AUG-2022, entry version 153.
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; Firmicutes; 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; P54616; -.
DR PRIDE; P54616; -.
DR EnsemblBacteria; CAB13029; CAB13029; BSU_11720.
DR GeneID; 939379; -.
DR KEGG; bsu:BSU11720; -.
DR PATRIC; fig|224308.179.peg.1261; -.
DR eggNOG; COG0623; Bacteria.
DR InParanoid; P54616; -.
DR OMA; GILDMIH; -.
DR PhylomeDB; P54616; -.
DR BioCyc; BSUB:BSU11720-MON; -.
DR BioCyc; MetaCyc:BSU11720-MON; -.
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:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
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 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 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
