ID Q03DJ1_PEDPA Unreviewed; 229 AA. AC Q03DJ1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 113. 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=PEPE_1710 {ECO:0000313|EMBL:ABJ68731.1}; OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / OS 183-1w). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ68731.1, ECO:0000313|Proteomes:UP000000773}; RN [1] {ECO:0000313|EMBL:ABJ68731.1, ECO:0000313|Proteomes:UP000000773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w RC {ECO:0000313|Proteomes:UP000000773}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P., RA Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). 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|ARBA:ARBA00000380, CC ECO:0000256|HAMAP-Rule:MF_01039, 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; CP000422; ABJ68731.1; -; Genomic_DNA. DR RefSeq; WP_002834107.1; NC_008525.1. DR AlphaFoldDB; Q03DJ1; -. DR STRING; 278197.PEPE_1710; -. DR GeneID; 33062508; -. DR KEGG; ppe:PEPE_1710; -. DR eggNOG; COG0588; Bacteria. DR HOGENOM; CLU_033323_1_1_9; -. DR OrthoDB; 9781415at2; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000773; 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; 2. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2. 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|HAMAP-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}. FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 87 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 8..15 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 21..22 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 87..90 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 114..115 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 183..184 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 182 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-3" SQ SEQUENCE 229 AA; 25898 MW; 85CCFDFD62997F4C CRC64; MAKLVLIRHG QSQWNLSNQF TGWVDVDLSD EGVKQAQNAG KLIKEAGIEF DQAYTSVLTR AIKTLHYALE GSDQLWIPET KTWRLNERHY GALQGQNKAE AAEKWGDDQV HTWRRSYDVL PPLLDADDEG SAANDRRYAN LDPRIIPGGE NLKVTLERVI PFWEDEIAPK LIDGKNVIIA AHGNSLRALS KYIENISDED IINLEMATGE PVVYDFNEKL EVQSKTKLN //