ID Q74GK6_GEOSL Unreviewed; 280 AA.
AC Q74GK6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN Name=fabD-1 {ECO:0000313|EMBL:AAR33574.1};
GN OrderedLocusNames=GSU0240 {ECO:0000313|EMBL:AAR33574.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR33574.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR33574.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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 Evidence={ECO:0000256|ARBA:ARBA00000936};
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DR EMBL; AE017180; AAR33574.1; -; Genomic_DNA.
DR RefSeq; NP_951301.1; NC_002939.5.
DR AlphaFoldDB; Q74GK6; -.
DR SMR; Q74GK6; -.
DR STRING; 243231.GSU0240; -.
DR EnsemblBacteria; AAR33574; AAR33574; GSU0240.
DR KEGG; gsu:GSU0240; -.
DR PATRIC; fig|243231.5.peg.239; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_4_1_7; -.
DR InParanoid; Q74GK6; -.
DR OrthoDB; 5393437at2; -.
DR Proteomes; UP000000577; 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; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..270
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 280 AA; 30832 MW; DC8FF0909195D1AA CRC64;
MICFMFPGQP LAPPVEFPED ADFEAIALLT RQRASFDLHT FSWTGEPSSD TVALQAYGVA
MGLYRTRRLR AEGIAPRLIA EHSMGIYPAL AAAGALDEGD ALELAVRLGR TMAAMGRQRT
YALGCMVGLT LEPLLVIAEN NGVYLANHNT SRHFLLAGER GAMEDACAEA LARGAFSARL
FPCDAPLHTP LMAEVAEELA AVAGDYRYRE PSVPLVDHID QDFLAAADLP VFMVRDLMEP
VRWERTYRAL RAAGVDRLYE VGAGDSLRKY NRWIESERGR
//
