ID GPMA_STRTD Reviewed; 230 AA. AC Q03KA9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 02-JUN-2021, entry version 85. 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}; OrderedLocusNames=STER_1172; OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=322159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-491 / LMD-9; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., 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.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; 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: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; CP000419; ABJ66363.1; -; Genomic_DNA. DR RefSeq; WP_011226119.1; NC_008532.1. DR SMR; Q03KA9; -. DR GeneID; 31937943; -. DR KEGG; ste:STER_1172; -. DR HOGENOM; CLU_033323_1_5_9; -. DR OMA; RMLPYWY; -. DR UniPathway; UPA00109; UER00186. 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; -; 1. DR HAMAP; MF_01039; PGAM_GpmA; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR005952; Phosphogly_mut1. DR PANTHER; PTHR11931; PTHR11931; 1. DR Pfam; PF00300; His_Phos_1; 2. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR TIGRFAMs; TIGR01258; pgm_1; 1. PE 3: Inferred from homology; KW Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1..230 FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate FT mutase" FT /id="PRO_1000064112" FT REGION 8..15 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT REGION 21..22 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT REGION 87..90 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT REGION 114..115 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT REGION 183..184 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT ACT_SITE 87 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 60 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 98 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT SITE 182 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" SQ SEQUENCE 230 AA; 26190 MW; F98CD5C6C0165EA7 CRC64; MVKLVFARHG ESEWNKANLF TGWADVDLSE KGTQQAIDAG KLIKEAGIEF DKAYTSVLKR AIKTTNLALE ASDQLWVPVE KSWRLNERHY GGLTGKNKAE AAEQFGDEQV HIWRRSYDVL PPKMDRDDEY SAHKDRRYAS LDDSVIPDAE NLKVTLERAL PFWEDKIAPA LKDGKNVFVG AHGNSIRALV KHIKKLSDDE IMDVEIPNFP PLVFEFDEKL NVVSEYYLGK //