ID C0R3S9_WOLWR Unreviewed; 506 AA. AC C0R3S9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038}; DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038}; GN Name=pgm {ECO:0000313|EMBL:ACN95571.1}; GN Synonyms=gpmI {ECO:0000256|HAMAP-Rule:MF_01038}; GN OrderedLocusNames=WRi_008330 {ECO:0000313|EMBL:ACN95571.1}; OS Wolbachia sp. subsp. Drosophila simulans (strain wRi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=66084 {ECO:0000313|EMBL:ACN95571.1, ECO:0000313|Proteomes:UP000001293}; RN [1] {ECO:0000313|EMBL:ACN95571.1, ECO:0000313|Proteomes:UP000001293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wRi {ECO:0000313|Proteomes:UP000001293}; RX PubMed=19307581; DOI=10.1073/pnas.0810753106; RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y., RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K., RA Andersson S.G.; RT "The mosaic genome structure of the Wolbachia wRi strain infecting RT Drosophila simulans."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; CC EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370, CC ECO:0000256|HAMAP-Rule:MF_01038}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01038}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01038}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798, CC ECO:0000256|HAMAP-Rule:MF_01038}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000256|ARBA:ARBA00008819, ECO:0000256|HAMAP- CC Rule:MF_01038}. 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; CP001391; ACN95571.1; -; Genomic_DNA. DR RefSeq; WP_007548604.1; NZ_MKIF01000051.1. DR AlphaFoldDB; C0R3S9; -. DR STRING; 66084.WRi_008330; -. DR KEGG; wri:WRi_008330; -. DR HOGENOM; CLU_026099_2_0_5; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000001293; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd16010; iPGM; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1. DR HAMAP; MF_01038; GpmI; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR011258; BPG-indep_PGM_N. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR036646; PGAM_B_sf. DR InterPro; IPR005995; Pgm_bpd_ind. DR NCBIfam; TIGR01307; pgm_bpd_ind; 1. DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1. DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF06415; iPGM_N; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001492; IPGAM; 1. DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01038}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01038}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01038}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01038}. FT DOMAIN 4..487 FT /note="Metalloenzyme" FT /evidence="ECO:0000259|Pfam:PF01676" FT DOMAIN 88..287 FT /note="BPG-independent PGAM N-terminal" FT /evidence="ECO:0000259|Pfam:PF06415" FT ACT_SITE 63 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-1" FT BINDING 12 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 151..152 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 182 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 253..256 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 323 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-2" FT BINDING 390 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 394 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 432 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 433 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" FT BINDING 451 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038, FT ECO:0000256|PIRSR:PIRSR001492-3" SQ SEQUENCE 506 AA; 55720 MW; F01D4F94B51C3FCB CRC64; MGIKSVVLCI LDGWGNGVEN SKYNAISNAN PPCWQYISSN YPKCSLSACG TDVGLPGGQI GNSEVGHMNI GSGRVVIQSL QRINQEIGTI ENNVNLQSFI SNLKSKNGVC HIMGLVSDGG VHSHQKHIST LANKISQHGI KVVIHAFLDG RDTLPNSGKK CIQEFIKSIK GNDIRIATVS GRYYAMDRDN RWERTIEAYE AIAFAKAPRH DNAVSLIDEN YQNNITDEFI RPAVIGDYQG IKPEDGVLLA NFRADRMIQL ASILLGKTDY AKVAKFSSIL SMMKYKKDLQ IPYIFPPTSF ADTLGQTIED NKLQQLRIAE TEKYAHVTFF FNCGKEEPFS GEERILIPSP KVQTYDLQPE MSAFELTEKL VEKIHSQEFA LIVVNYANPD MVGHTGNIKA AEKAVLAVDD CLAKVLSAVK KSSNTALIVT ADHGNVECMF DEENNTPHTA HTLNKVPFIV SCDNLKLRDG RLSDIAPTIL QLLGIKKPDE MTGSSLISCI TLCHSS //