ID Q82JS3_STRAW Unreviewed; 266 AA.
AC Q82JS3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:BAC70392.1};
GN Name=plsC2 {ECO:0000313|EMBL:BAC70392.1};
GN ORFNames=SAVERM_2681 {ECO:0000313|EMBL:BAC70392.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC70392.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC70392.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC70392.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
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DR EMBL; BA000030; BAC70392.1; -; Genomic_DNA.
DR RefSeq; WP_010984113.1; NZ_JZJK01000071.1.
DR AlphaFoldDB; Q82JS3; -.
DR KEGG; sma:SAVERM_2681; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_1_11; -.
DR OrthoDB; 9806008at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000428}.
FT DOMAIN 41..159
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 221..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 30035 MW; 1A973FAB82BCDB4F CRC64;
MPRRRISFWY RFAAVLCKPP LVVLIKRDWR GMENIPVEGG FITAVNHNSH VDPFAYAHYQ
YNTGRVPRFL AKAGLFKKGF VGAAMRGTGQ IPVYRESTDA LSAFRAAIDA VERGECVAFY
PEGTLTRDPD GWPMTGKTGA ARVALQTKCP VIPVAQWGAN ELLPPYAKKP NLLPRKTHRV
LAGPPVDLTR FYDREMSPDL LKEATEVIMA AVTAQLEEIR GEKAPERPYD PRQVRIEQRR
RTAAYERAQA QQKAQQRAQQ EEEQST
//
