ID A0A0N9N4C0_9ACTN Unreviewed; 303 AA.
AC A0A0N9N4C0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ACH46_13010 {ECO:0000313|EMBL:ALG85228.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG85228.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG85228.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG85228.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG85228.1; -; Genomic_DNA.
DR RefSeq; WP_062393301.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9N4C0; -.
DR STRING; 1136941.ACH46_13010; -.
DR KEGG; goq:ACH46_13010; -.
DR PATRIC; fig|1136941.3.peg.2649; -.
DR OrthoDB; 3248271at2; -.
DR Proteomes; UP000063789; Chromosome.
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, ECO:0000313|EMBL:ALG85228.1}.
FT DOMAIN 5..295
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 303 AA; 31467 MW; 4971DF7C18CADD80 CRC64;
MLSLLAPGQG SQKPGMLAEW LELPGARDRV ATWSDITGLD LERLGTTATA EEITDTAVTQ
PLVVAGALLS FDEIRKRHGE LPADTVIAGH SIGEVAAAAI AGVITFDEAM MLAGVRGAEM
AKACSLEATT MAAVLGGDED VVLAHLSSLD LVPANRNAKG QIVAAGAVSA IEELIANPPE
KARTRQLAVA GAFHTRYMAP AQDAFAEAAA QIDPADPNRA LLSNADGKTV ISGVETIKRL
VMQVTSPVRW DLCSETLRES EATGIIELAP GGTLVGIAKR EMKGVPARAV KVPGDLEDLP
ELG
//
