ID A0A0H3MQW2_MYCLB Unreviewed; 329 AA. AC A0A0H3MQW2; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 03-MAY-2023, entry version 27. DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635}; GN OrderedLocusNames=MLBr01423 {ECO:0000313|EMBL:CAR71518.1}; OS Mycobacterium leprae (strain Br4923). OC Bacteria; Actinomycetota; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=561304 {ECO:0000313|EMBL:CAR71518.1, ECO:0000313|Proteomes:UP000006900}; RN [1] {ECO:0000313|EMBL:CAR71518.1, ECO:0000313|Proteomes:UP000006900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Br4923 {ECO:0000313|Proteomes:UP000006900}; RX PubMed=19881526; DOI=10.1038/ng.477; RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R., RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A., RA Rougemont J., Brennan P.J., Cole S.T.; RT "Comparative genomic and phylogeographic analysis of Mycobacterium RT leprae."; RL Nat. Genet. 41:1282-1289(2009). 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; FM211192; CAR71518.1; -; Genomic_DNA. DR RefSeq; WP_010908332.1; NC_011896.1. DR AlphaFoldDB; A0A0H3MQW2; -. DR EnsemblBacteria; CAR71518; CAR71518; MLBr01423. DR KEGG; mlb:MLBr01423; -. DR HOGENOM; CLU_047251_3_0_11; -. DR OMA; IDYNKFT; -. DR Proteomes; UP000006900; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07207; Pat_ExoU_VipD_like; 1. DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR002641; PNPLA_dom. DR PANTHER; PTHR46394; ANNEXIN; 1. DR PANTHER; PTHR46394:SF1; PNPLA DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR PROSITE; PS51635; PNPLA; 1. PE 4: Predicted; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161}; KW Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE- KW ProRule:PRU01161}. FT DOMAIN 14..213 FT /note="PNPLA" FT /evidence="ECO:0000259|PROSITE:PS51635" FT MOTIF 18..23 FT /note="GXGXXG" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT MOTIF 45..49 FT /note="GXSXG" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT MOTIF 200..202 FT /note="DGA/G" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT ACT_SITE 47 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT ACT_SITE 200 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" SQ SEQUENCE 329 AA; 35485 MW; ED9B639250EDAEEB CRC64; MLYLVIVSVV HADLVCQGGG IRGIGLVGAV DALATAGYRF PRVAGTSAGA LVASLIAALQ TAGEPLTRLA EVMRTIDYRK FFDRSLIGRV PLIGGGLSLL VSDGVYQGAY LEEWLTSLLG DLGVYTFGDL RTGEEPEQFA WSLVVTASDL SRRRLVRIPW DLDAYGINPD DFSVARAVHA SSAIPYVFEP VQVAGATWVD GGLLSTFPVE LFDRSDGDAR WPTFGIRLSA RPGIPPTHPV RGPVSLGIAA IETLVSNQDN AYIDDSCTML RTIFVPADEV SPIDFNITVE QRQALYQSGL QAGQQFLKTW NYTEYLTACG RPVTRSAGL //