ID GPMI_HELPY Reviewed; 491 AA. AC P56196; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038}; DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038}; DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038}; GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm; GN OrderedLocusNames=HP_0974; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01038}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01038}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01038}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01038}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000255|HAMAP-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; AE000511; AAD08020.1; -; Genomic_DNA. DR PIR; F64641; F64641. DR RefSeq; NP_207765.1; NC_000915.1. DR RefSeq; WP_000057737.1; NC_018939.1. DR AlphaFoldDB; P56196; -. DR SMR; P56196; -. DR DIP; DIP-3166N; -. DR IntAct; P56196; 1. DR MINT; P56196; -. DR STRING; 85962.HP_0974; -. DR PaxDb; 85962-C694_05010; -. DR EnsemblBacteria; AAD08020; AAD08020; HP_0974. DR KEGG; hpy:HP_0974; -. DR PATRIC; fig|85962.47.peg.1042; -. DR eggNOG; COG0696; Bacteria. DR InParanoid; P56196; -. DR OrthoDB; 9800863at2; -. DR PhylomeDB; P56196; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. 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; Isomerase; Manganese; Metal-binding; Reference proteome. FT CHAIN 1..491 FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate FT mutase" FT /id="PRO_0000212154" FT ACT_SITE 61 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 11 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 61 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 147..148 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 247..250 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 386 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 390 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 427 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 428 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" FT BINDING 445 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038" SQ SEQUENCE 491 AA; 54788 MW; F72F8CDA04EA9D6D CRC64; MAQKTLLIIT DGIGYRKDSD HNAFFHAKKP TYDLMFKTLP YSLIDTHGLS VGLPKGQMGN SEVGHMCIGA GRVLYQDLVK ISLSLQNDEL KNNPAFLNTI QKSPVVHLMG LMSDGGVHSH IEHFIALALE CEKSHKKVCL HLITDGRDVA PKSALTYLKQ MQNICNESIQ IATISGRFYA MDRDKRFERI ELAYHSLMGL NHTPLSPSEY IQSQYDKNIT DEFIMPACFK NYCGMQDDES FIFINFRNDR AREIVSALGQ KQFSGFKRQV FKKLHIATMT PYDNTFPYPV LFPKESVQNT LAEVVSQHNL TQSHIAETEK YAHVTFFING GVETPFKNEN RVLIQSPKVT TYDLKPEMSA KEVTLAVLEQ MKLGTDLIIV NFANGDMVGH TGNFEASVKA VEAVDACLGE ILSLAKKLDY AMLLTSDHGN CERMKDENQN PLTNHTAGSV YCFVLGDGVK SIKNGALNNI ASSVLKLMGL KAPATMDEPL F //