ID A0A0D2J743_9EURO Unreviewed; 385 AA.
AC A0A0D2J743;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN ORFNames=Z518_05776 {ECO:0000313|EMBL:KIX04905.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX04905.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX04905.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX04905.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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};
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DR EMBL; KN847478; KIX04905.1; -; Genomic_DNA.
DR RefSeq; XP_013272041.1; XM_013416587.1.
DR AlphaFoldDB; A0A0D2J743; -.
DR STRING; 1442369.A0A0D2J743; -.
DR GeneID; 25293847; -.
DR VEuPathDB; FungiDB:Z518_05776; -.
DR HOGENOM; CLU_030558_5_0_1; -.
DR OrthoDB; 2265421at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..368
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 385 AA; 42693 MW; DE6F663FC8E66A42 CRC64;
MYRPTYTGLR GLKQILPRPS RTYGTTPEPT LRTALFFPGH GVQRKGMTRP WVEAFPRTCK
PFLEEMDEIV QCKLSTLIDE GPILQLDKTE NAQPAIMAVS IMILRVLEQE FGFKTDEVID
VTLGHSLGEY AALVAAGNLE YAFALDLVRR RGDVMGECTR KAKEESGEDF GMIALVCEPD
QLDSLIAAVK EFLSHGAEGA KDDSSALPAI QQVAIANANS KNQIVLSGSF QRIRNLLVHI
REFGGHDPRA VELKSRSAFH SPIMMPAYEF MKKALTPDMV TFPGRVPCIS NVTARPFSSK
EDLIQNLARQ AVDTILWWDS IKYLDRQAGC RRYLGVGPGK VGRNLVSKEV GRSSAKGGGV
WSITEPHEIE DTLRELEATA KEEDK
//
