ID A0A067BW59_SAPPC Unreviewed; 958 AA.
AC A0A067BW59;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=SPRG_16133 {ECO:0000313|EMBL:KDO18531.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO18531.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO18531.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO18531.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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DR EMBL; KK583422; KDO18531.1; -; Genomic_DNA.
DR RefSeq; XP_012210756.1; XM_012355366.1.
DR AlphaFoldDB; A0A067BW59; -.
DR EnsemblProtists; KDO18531; KDO18531; SPRG_16133.
DR GeneID; 24137785; -.
DR KEGG; spar:SPRG_16133; -.
DR VEuPathDB; FungiDB:SPRG_16133; -.
DR OrthoDB; 67806at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF02450; LCAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030745}.
FT DOMAIN 99..393
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 958 AA; 104818 MW; 985E41A875A534CB CRC64;
MPARFHYLFP LASDDLHAAV TAVLPTLEAS VLAKGNASLA ELYRTWSFAD RGASRLVVRA
STLRELLNGL RSFLNGCPEP DVVFVATSVP ATPPPLVCIF NGMGGQWNGM GATLNEVYPV
FASALTAAEE ALLAVAGGAR FVPAMLDPSS TSMTTNAGAQ AGNFVLQVAL LAELSSRLVA
PYMGALGLSA GEPAAAYAAG SLSLSDAAKV VCTRLAMQDR VAAHDGGMLA IRASEAIITP
LLPAEVEVAA VLSPHLSTVT GPIQALETLK TTLPASILTI DLPMRAAYHS RVMEQANIPT
DLVVALQDLR PRPPTTARLF STVTGGEIAT LLDAAYWYAN VRQPVLFQSA VETALRAGGA
VFVELGPHAS IARSIEFIAG ASASSVPSML RGTEELLQLD RATIHLYLHG HVIQLVLAAV
GLVAATASPK RQVLPVVLIP GLASSQLHAW KNERCHGSIG QEVKIGDRMW IDVGRLLSQT
DCWERCMRLH TRNQSDVACK LRAGDGISAI TELAPGLVTG PLSVVWRHVI ETLTGHFDMG
PHQLMVAAYD WRLPPSMLQE RDHFFYTMLK RIEDAVHLHQ SRGVVIIAHS LGNNVLRYFL
AWVKHHIHLT DDVHEAWVRR HIAAYFALGT PFLGSSEPLE CLVTGLSVKM PLSLDMYRRL
QTSHGSTQWI LPIPRTLHDD PTDAQAQQAF ASVTYPGEAG STVTRSFSMR ELTNGSFHRA
MAARDPTFED LEYVRERYYA QDPVLNVHTP WTRPPIESIY VIYGTGKKVR HRYTYTERER
GAWTLDELFT ETPDAATCNK TGDGTVSYYS LSWGHTWLGA DGDSVTMTRA PQAPYFSRKD
IAQTKATRVK YAEYQGGLQC KSSESPSLAS AETQAMQMHY NSGFLSDLWS SASDEPRIHF
FEHSGVSPTG RSLHTSVWEF DLIQHREMLS EPAFLRELKF ELHNVFDGKA HTDKFYPR
//