FABG_BACSU
ID FABG_BACSU Reviewed; 246 AA.
AC P51831; O31733;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG;
DE EC=1.1.1.100;
DE AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase;
DE AltName: Full=Beta-ketoacyl-ACP reductase;
GN Name=fabG; Synonyms=ylpF; OrderedLocusNames=BSU15910;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8759840; DOI=10.1128/jb.178.16.4794-4800.1996;
RA Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.;
RT "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid
RT biosynthesis genes.";
RL J. Bacteriol. 178:4794-4800(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172.
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-246.
RC STRAIN=168;
RX PubMed=8654983; DOI=10.1016/0378-1119(96)00181-3;
RA Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.;
RT "The effect of Srb, a homologue of the mammalian SRP receptor alpha-
RT subunit, on Bacillus subtilis growth and protein translocation.";
RL Gene 172:17-24(1996).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC in the elongation cycle of fatty acid biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U59433; AAC44307.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13464.1; -; Genomic_DNA.
DR EMBL; Y13937; CAA74250.1; -; Genomic_DNA.
DR EMBL; D64116; BAA10974.1; -; Genomic_DNA.
DR PIR; A69621; A69621.
DR RefSeq; NP_389473.1; NC_000964.3.
DR RefSeq; WP_003232035.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P51831; -.
DR SMR; P51831; -.
DR IntAct; P51831; 1.
DR MINT; P51831; -.
DR STRING; 224308.BSU15910; -.
DR jPOST; P51831; -.
DR PaxDb; P51831; -.
DR PRIDE; P51831; -.
DR EnsemblBacteria; CAB13464; CAB13464; BSU_15910.
DR GeneID; 938113; -.
DR KEGG; bsu:BSU15910; -.
DR PATRIC; fig|224308.179.peg.1731; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P51831; -.
DR OMA; KMPERDY; -.
DR PhylomeDB; P51831; -.
DR BioCyc; BSUB:BSU15910-MON; -.
DR BioCyc; MetaCyc:BSU15910-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR InterPro; IPR011284; 3oxo_ACP_reduc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..246
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT /id="PRO_0000054665"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 62..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="D -> A (in Ref. 1; AAC44307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26282 MW; C6A391167D3237DC CRC64;
MLNDKTAIVT GASRGIGRSI ALDLAKSGAN VVVNYSGNEA KANEVVDEIK SMGRKAIAVK
ADVSNPEDVQ NMIKETLSVF STIDILVNNA GITRDNLIMR MKEDEWDDVI NINLKGVFNC
TKAVTRQMMK QRSGRIINVS SIVGVSGNPG QANYVAAKAG VIGLTKSSAK ELASRNITVN
AIAPGFISTD MTDKLAKDVQ DEMLKQIPLA RFGEPSDVSS VVTFLASEGA RYMTGQTLHI
DGGMVM
