ID O53516_MYCTU Unreviewed; 247 AA. AC O53516; F2GJY9; I6YCR4; Q7D7E3; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 145. DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:CCP44959.1}; GN OrderedLocusNames=Rv2182c {ECO:0000313|EMBL:CCP44959.1}; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP44959.1, ECO:0000313|Proteomes:UP000001584}; RN [1] {ECO:0000313|EMBL:CCP44959.1, ECO:0000313|Proteomes:UP000001584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584}; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., RA Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] {ECO:0007829|PubMed:21969609} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21969609; DOI=10.1074/mcp.M111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). 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; AL123456; CCP44959.1; -; Genomic_DNA. DR RefSeq; NP_216698.1; NC_000962.3. DR RefSeq; WP_003411341.1; NZ_NVQJ01000008.1. DR AlphaFoldDB; O53516; -. DR SMR; O53516; -. DR STRING; 83332.Rv2182c; -. DR PaxDb; 83332-Rv2182c; -. DR DNASU; 888625; -. DR GeneID; 45426158; -. DR GeneID; 888625; -. DR KEGG; mtu:Rv2182c; -. DR PATRIC; fig|83332.111.peg.2429; -. DR TubercuList; Rv2182c; -. DR eggNOG; COG0204; Bacteria. DR InParanoid; O53516; -. DR OrthoDB; 9808424at2; -. DR PhylomeDB; O53516; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. 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 1: Evidence at protein level; KW Reference proteome {ECO:0000313|Proteomes:UP000001584}. FT DOMAIN 35..154 FT /note="Phospholipid/glycerol acyltransferase" FT /evidence="ECO:0000259|SMART:SM00563" FT REGION 226..247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 247 AA; 26955 MW; FB1094228A340BDB CRC64; MWYYLFKYIF MGPLFTLLGR PKVEGLEYIP SSGPAILASN HLAVADSFYL PLVVRRRIWF LAKSEYFTGT GLKGWINRWF YSVSGQVPID RTNADSAQGA LQTAVVLLGQ GKLLGMYPEG TRSPDGRLYK GKTGLARLAL HTGVPVIPVA MIGTNVVNPP GRKMLRFGRV TVRFGKPMDF SRFEGLAGNH FIERAVTDEV IYELMGLSGQ EYVDIYAASV KDGRNAGGAG ANPNSTDAAR IPETAAG //