ID GPMA_STRGG Reviewed; 253 AA. AC B1VS80; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 24-JAN-2024, entry version 81. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039}; DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039}; GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; GN OrderedLocusNames=SGR_4005; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350; RX PubMed=18375553; DOI=10.1128/jb.00204-08; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "Genome sequence of the streptomycin-producing microorganism Streptomyces RT griseus IFO 13350."; RL J. Bacteriol. 190:4050-4060(2008). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; CC EC=5.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01039}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01039}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}. 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; AP009493; BAG20834.1; -; Genomic_DNA. DR RefSeq; WP_003968178.1; NC_010572.1. DR AlphaFoldDB; B1VS80; -. DR SMR; B1VS80; -. DR GeneID; 6214098; -. DR KEGG; sgr:SGR_4005; -. DR eggNOG; COG0588; Bacteria. DR HOGENOM; CLU_033323_1_1_11; -. DR OMA; RMLPYWY; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd07067; HP_PGM_like; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1. DR HAMAP; MF_01039; PGAM_GpmA; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR001345; PG/BPGM_mutase_AS. DR InterPro; IPR005952; Phosphogly_mut1. DR NCBIfam; TIGR01258; pgm_1; 1. DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1. DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF00300; His_Phos_1; 1. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 3: Inferred from homology; KW Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1..253 FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate FT mutase" FT /id="PRO_1000135980" FT ACT_SITE 13 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT ACT_SITE 91 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 12..19 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 25..26 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 91..94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 118..119 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 187..188 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT SITE 186 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" SQ SEQUENCE 253 AA; 28425 MW; 805B19AE803FD97C CRC64; MADAPYKLIL LRHGESEWNA KNLFTGWVDV NLTEKGEKEA VRGGELLKDA GLLPDVLHTS LQRRAIRTAQ LALESADRLW IPVRRSWRLN ERHYGALQGK DKAQTLAEFG EEQFMLWRRS YDTPPPPLAR DDEFSQFDDP RYATLPPEVR PDTECLKDVV VRMLPYWFDS IVPDLLTGRT VLVAAHGNSL RGLVKHLDGI SDEDISGLNI PTGIPLSYEL DADFKPLKPG GTYLDPDAAK AAIEAVKNQG KKK //