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 15-MAR-2017, entry version 71. 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=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., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA 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 CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {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 ProteinModelPortal; Q03KA9; -. DR SMR; Q03KA9; -. DR EnsemblBacteria; ABJ66363; ABJ66363; STER_1172. DR GeneID; 3165581; -. DR KEGG; ste:STER_1172; -. DR PATRIC; 19799690; VBIStrThe129203_1196. DR HOGENOM; HOG000221682; -. DR KO; K01834; -. DR OMA; VKNQGKK; -. DR UniPathway; UPA00109; UER00186. DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. 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 2,3-bisphosphoglycerate-dependent FT phosphoglycerate mutase. FT /FTId=PRO_1000064112. FT REGION 8 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 21 22 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 87 90 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 114 115 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 183 184 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT ACT_SITE 9 9 Tele-phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT ACT_SITE 87 87 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT BINDING 60 60 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT BINDING 98 98 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT SITE 182 182 Transition state stabilizer. FT {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 //