FABD_BACSU
ID FABD_BACSU Reviewed; 317 AA.
AC P71019; O34463;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE Short=MCT;
DE EC=2.3.1.39;
GN Name=fabD; Synonyms=ylpE; OrderedLocusNames=BSU15900;
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 [GENOMIC DNA].
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 [3]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR EMBL; U59433; AAC44306.1; -; Genomic_DNA.
DR EMBL; Y13937; CAA74249.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13463.1; -; Genomic_DNA.
DR PIR; H69620; H69620.
DR RefSeq; NP_389472.1; NC_000964.3.
DR RefSeq; WP_003245314.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P71019; -.
DR SMR; P71019; -.
DR IntAct; P71019; 1.
DR MINT; P71019; -.
DR STRING; 224308.BSU15900; -.
DR jPOST; P71019; -.
DR PaxDb; P71019; -.
DR EnsemblBacteria; CAB13463; CAB13463; BSU_15900.
DR GeneID; 938488; -.
DR KEGG; bsu:BSU15900; -.
DR PATRIC; fig|224308.179.peg.1730; -.
DR eggNOG; COG0331; Bacteria.
DR InParanoid; P71019; -.
DR OMA; AANYNCP; -.
DR PhylomeDB; P71019; -.
DR BioCyc; BSUB:BSU15900-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.366.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR PIRSF; PIRSF000446; Mct; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR00128; fabD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Malonyl CoA-acyl carrier protein transacylase"
FT /id="PRO_0000194210"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /evidence="ECO:0000250"
FT CONFLICT 124..131
FT /note="VPAGEGAM -> GCRLAKEQW (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 34035 MW; 191AE828B1C91D7F CRC64;
MSKIAFLFPG QGSQFIGMGK ELYEQVPAAK RLFDEADETL ETKLSSLIFE GDAEELTLTY
NAQPALLTTS IAVLEKFKES GITPDFTAGH SLGEYSALVA AGALSFKDAV YTVRKRGEFM
NEAVPAGEGA MAAILGMDAE ALKQVTDKVT EEGNLVQLAN LNCPGQIVIS GTAKGVELAS
ELAKENGAKR AIPLEVSGPF HSELMKPAAE KLKEVLDACD IKDADVPVIS NVSADVMTEK
ADIKEKLIEQ LYSPVRFEES INKLIAEGVT TFIEIGPGKV LSGLVKKVNR RLKTIAVSDP
ETIELAIQTL KEENDNA