ID A7HYI1_PARL1 Unreviewed; 313 AA.
AC A7HYI1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|ARBA:ARBA00018953, ECO:0000256|PIRNR:PIRNR000446};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258, ECO:0000256|PIRNR:PIRNR000446};
GN OrderedLocusNames=Plav_3360 {ECO:0000313|EMBL:ABS64964.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS64964.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS64964.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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,
CC ECO:0000256|PIRNR:PIRNR000446};
CC -!- SIMILARITY: Belongs to the fabD family.
CC {ECO:0000256|PIRNR:PIRNR000446}.
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DR EMBL; CP000774; ABS64964.1; -; Genomic_DNA.
DR RefSeq; WP_012112295.1; NC_009719.1.
DR AlphaFoldDB; A7HYI1; -.
DR STRING; 402881.Plav_3360; -.
DR KEGG; pla:Plav_3360; -.
DR eggNOG; COG0331; Bacteria.
DR HOGENOM; CLU_030558_0_1_5; -.
DR OrthoDB; 9808564at2; -.
DR Proteomes; UP000006377; Chromosome.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR NCBIfam; TIGR00128; fabD; 1.
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 PIRSF; PIRSF000446; Mct; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000446};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000446}.
FT DOMAIN 6..306
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
FT ACT_SITE 204
FT /evidence="ECO:0000256|PIRSR:PIRSR000446-1"
SQ SEQUENCE 313 AA; 32493 MW; 3DE70837A49C28FA CRC64;
MSRAFTFPGQ GSQAVGMGRE LAEAFAPARE VFDEVNDALG ENLSKLMWEG PQEELTLTEN
AQPAIMAVSL AVIRTLEREG GFSLAGKAAF VAGHSLGEYS ALAAAGAFTL ADTARLLKRR
GLAMQRAVPV GEGAMAALLG LEFEQAAEVA AEAAQGEVCA AANDNGGGQV VVSGAKAAVE
RAIEIAKTKG AKRSMLLPVS APFHCSLMQP AADEMAEALA AVDIKAPSVP LVANVTASRV
ADPATIRDLL VQQVTGMVRW RESVLYMEAQ GVVNFVEVGA GKALSGMVKR IVKEADLVSV
GTPADVEAFL KTL
//
