ID Q9S2M2_STRCO Unreviewed; 262 AA. AC Q9S2M2; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563}; GN OrderedLocusNames=SCO2122 {ECO:0000313|EMBL:CAB51970.1}; GN ORFNames=SC6E10.16c {ECO:0000313|EMBL:CAB51970.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB51970.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB51970.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H., RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL939111; CAB51970.1; -; Genomic_DNA. DR PIR; T35503; T35503. DR RefSeq; NP_626379.1; NC_003888.3. DR AlphaFoldDB; Q9S2M2; -. DR STRING; 100226.gene:17759720; -. DR PaxDb; 100226-SCO2122; -. DR PATRIC; fig|100226.15.peg.2157; -. DR eggNOG; COG0204; Bacteria. DR HOGENOM; CLU_027938_4_0_11; -. DR InParanoid; Q9S2M2; -. DR OrthoDB; 9808424at2; -. DR PhylomeDB; Q9S2M2; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central. 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:UP000001973}. FT DOMAIN 34..155 FT /note="Phospholipid/glycerol acyltransferase" FT /evidence="ECO:0000259|SMART:SM00563" FT REGION 234..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..255 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 262 AA; 28171 MW; D30E925B49D14A47 CRC64; MLYGAMKVTV GGSLKLAFRP WVEGLEHIPA DGPAILASNH LSFSDSFFLP AVLDRKVTFI AKAEYFNTPG VKGRLTAAFF KGVGQLPVDR SGARGAGEAA IKSGIEVLER GELFGIYPEG TRSPDGRLYR GKPGGLARVA LATGAPVVPV AMIDTEKIQP PGQVMPKLMR PGIRIGKPLD FSRYQGMEHD RFVLRAVTDE VMYEIMKLSG QEYVDMYATA MKRQLAEAAK AEKAAKAEKA AKNDKAAKND KAAKAGTDRA GT //