ID C7MSY8_SACVD Unreviewed; 249 AA. AC C7MSY8; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 28-JAN-2026, entry version 93. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512}; DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039}; DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512}; GN Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039}; GN OrderedLocusNames=Svir_02670 {ECO:0000313|EMBL:ACU95349.1}; OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / CCUG OS 5913 / NBRC 12207 / NCIMB 9602 / P101) (Thermoactinomyces viridis). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95349.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU95349.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; DOI=10.4056/sigs.20263; RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D., RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N., RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Saccharomonospora viridis type strain RT (P101)."; RL Stand. Genomic Sci. 1:141-149(2009). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}. 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:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717, CC ECO:0000256|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; CP001683; ACU95349.1; -; Genomic_DNA. DR RefSeq; WP_012795782.1; NC_013159.1. DR AlphaFoldDB; C7MSY8; -. DR STRING; 471857.Svir_02670; -. DR KEGG; svi:Svir_02670; -. DR eggNOG; COG0588; Bacteria. DR HOGENOM; CLU_033323_1_1_11; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000841; Chromosome. DR GO; GO:0004619; F: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 FunFam; 3.40.50.1240:FF:000012; Phosphoglycerate mutase 1; 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 NCBIfam; NF010713; PRK14115.1; 1. DR NCBIfam; NF010718; PRK14120.1; 1. DR PANTHER; PTHR11931; 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 {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP- KW Rule:MF_01039}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01039}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}; KW Reference proteome {ECO:0000313|Proteomes:UP000000841}. FT ACT_SITE 12 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 90 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 11..18 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 24..25 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 63 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 90..93 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 101 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 117..118 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 185..186 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 184 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-3" SQ SEQUENCE 249 AA; 27566 MW; E875F3CE2A1917E3 CRC64; MAELGTLVLL RHGQSTWNAE NLFTGWVDVP LSEQGEAEAR RGGELLAEAG LLPDVVHTSL LRRAISTANI ALDVADRHWI DVRRDWRLNE RHYGALQGKN KKETLEQFGE EQFMLWRRSY DTPPPPIEPG SQYSQDGDVR YADLGDKLPT TECLKDVVER LLPYWESAIV PDLRAGKTVL IAAHGNSLRA LVKHLDGISD EDIVGLNIPT GIPLRYDLDE NLKPTNPGGT YLDPEAAEKA AAAVASQGR //