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Database: UniProt
Entry: S3DBQ0_GLAL2
LinkDB: S3DBQ0_GLAL2
Original site: S3DBQ0_GLAL2 
ID   S3DBQ0_GLAL2            Unreviewed;       421 AA.
AC   S3DBQ0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=[acyl-carrier-protein] S-malonyltransferase {ECO:0000256|ARBA:ARBA00013258};
DE            EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
GN   ORFNames=GLAREA_10233 {ECO:0000313|EMBL:EPE34539.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE34539.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE34539.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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; KE145356; EPE34539.1; -; Genomic_DNA.
DR   RefSeq; XP_008078474.1; XM_008080283.1.
DR   AlphaFoldDB; S3DBQ0; -.
DR   STRING; 1116229.S3DBQ0; -.
DR   GeneID; 19469280; -.
DR   KEGG; glz:GLAREA_10233; -.
DR   eggNOG; KOG2926; Eukaryota.
DR   HOGENOM; CLU_030558_5_0_1; -.
DR   OMA; AANYNCP; -.
DR   OrthoDB; 2265421at2759; -.
DR   Proteomes; UP000016922; 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:UP000016922};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          57..403
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
SQ   SEQUENCE   421 AA;  46636 MW;  61C85FAB87E97C11 CRC64;
     MRSLATGLPK RCRYAPRRQL PREVSHGTCL TRQQPISNHI QVRHASTKPH RPRTAIFFPG
     QGVQRVGMLT PWLEAFPATA KPAVEEIDHL LGYKLSTIIE EGPNSLLTAT GNAQPAIMAS
     SLLILRILER EFGFQTAERV DVTLGHSLGE FAALVAGGFV QFEDSLYLVR KRAELMAESS
     QKAREEFGGD YGMIALVTEP NHLASLIDSI HEFLGYHSAG SKSESALDVP PIQQVLIANI
     NSKNQIVLSG NIAAIKQLLT HIRQFGGHDP RAVRLKSDSP FHSPLMKPAA TAMRKLLDGK
     SRVKGKEDQD IVTFPGKMEC ISNVSARPFT GAEDLKDLWA RQCVETVRWW DSIKYLDQEQ
     KVRRWIGIGP GKVGRNLVGK EVGMRGRDVV KGGGVWGISD PKEIEEMLKA LDDTENIRDD
     E
//
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