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Database: UniProt
Entry: R5QEM3_9BURK
LinkDB: R5QEM3_9BURK
Original site: R5QEM3_9BURK 
ID   R5QEM3_9BURK            Unreviewed;       301 AA.
AC   R5QEM3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   ORFNames=BN489_00603 {ECO:0000313|EMBL:CCZ19537.1};
OS   Sutterella wadsworthensis CAG:135.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=1263111 {ECO:0000313|EMBL:CCZ19537.1, ECO:0000313|Proteomes:UP000018089};
RN   [1] {ECO:0000313|EMBL:CCZ19537.1, ECO:0000313|Proteomes:UP000018089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:135 {ECO:0000313|Proteomes:UP000018089};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCZ19537.1}.
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DR   EMBL; CAZN010000487; CCZ19537.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QEM3; -.
DR   Proteomes; UP000018089; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..290
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   301 AA;  32089 MW;  FFB51727AA8CEECE CRC64;
     MRVFFVFPGQ GTQRPGILHG LNTFGLSVLE EMSNAIGLDL LTLDSAEAFE RTENVQLALL
     CAGIGKCREL EAAGIQPSLV AGLSIGAFGA AVAAHALSLT DAARLVLLRG RLMQGAYPSG
     YGMMAIGGLN LNTAEDITNA VDDIYVSNIN SEQQIVLSGP LSSLDIAAKR AKDRGALYAK
     RIQVTVPSHC PLLMCPAKVL MEAFQKVEVK RPKVPYLSVN SGRVIWDPTK LVDDLAFNMA
     RRTSWLDAAQ AAKERGIDVL IEMPPGGILG SLAKTTFADG LVISSSTTPA EEIIERIGRL
     Q
//
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