ID A0A9W3JU01_BACTU Unreviewed; 190 AA. AC A0A9W3JU01; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 24-JUL-2024, entry version 5. DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:AFQ27763.1}; GN ORFNames=BTF1_17970 {ECO:0000313|EMBL:AFQ27763.1}; OS Bacillus thuringiensis HD-789. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1217737 {ECO:0000313|EMBL:AFQ27763.1, ECO:0000313|Proteomes:UP000005257}; RN [1] {ECO:0000313|EMBL:AFQ27763.1, ECO:0000313|Proteomes:UP000005257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HD-789 {ECO:0000313|EMBL:AFQ27763.1, RC ECO:0000313|Proteomes:UP000005257}; RX PubMed=24309743; RA Doggett N.A., Stubben C.J., Chertkov O., Bruce D.C., Detter J.C., RA Johnson S.L., Han C.S.; RT "Complete Genome Sequence of Bacillus thuringiensis Serovar Israelensis RT Strain HD-789."; RL Genome Announc. 1:e01023-e01013(2013). 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; CP003763; AFQ27763.1; -; Genomic_DNA. DR RefSeq; WP_000134944.1; NC_018508.1. DR SMR; A0A9W3JU01; -. DR GeneID; 67468120; -. DR KEGG; btn:BTF1_17970; -. DR Proteomes; UP000005257; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0016791; F:phosphatase activity; IEA:TreeGrafter. DR CDD; cd07067; HP_PGM_like; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR001345; PG/BPGM_mutase_AS. DR InterPro; IPR050275; PGM_Phosphatase. DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1. DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1. DR Pfam; PF00300; His_Phos_1; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 4: Predicted; FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 83 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 8..15 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 58 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" SQ SEQUENCE 190 AA; 21131 MW; FD22CDCE5A3FAD19 CRC64; MTEICLVRHG QTDWNFQEII QGREDIPLNE VGKKQASQSA AALQEETWDI IISSPLIRAQ ETANEIAKAA GLQSILLDDR FVERNFGEAS GKPVATVREL IAEGKVEGME QDEEIVARCF AALEDVATTH FGKRIIIVAH SHAIKAILHA IEPDEITFKT PLKNACISYV KQNSGKWDVL KYNIAEHINV //