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 03-NOV-2009, entry version 21. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; DE Short=Phosphoglyceromutase; DE Short=PGAM; DE Short=BPG-dependent PGAM; DE Short=dPGM; DE EC=5.4.2.1; GN Name=gpmA; OrderedLocusNames=STER_1172; OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=322159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. 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; YP_820559.1; -. DR STRING; Q03KA9; -. DR GeneID; 4438655; -. DR GenomeReviews; CP000419_GR; STER_1172. DR KEGG; ste:STER_1172; -. DR OMA; FMLWRRS; -. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphogl...; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR HAMAP; MF_01039; -; 1. DR InterPro; IPR001345; PG/BPGM_mutase_AC. DR InterPro; IPR013078; PG_mutase. DR InterPro; IPR005952; Phosphogly_mut1. DR PANTHER; PTHR11931; Phosphogly_mut1; 1. DR Pfam; PF00300; PGAM; 1. DR TIGRFAMs; TIGR01258; pgm_1; 1. DR PROSITE; PS00175; PG_MUTASE; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Isomerase. FT CHAIN 1 230 2,3-bisphosphoglycerate-dependent FT phosphoglycerate mutase. FT /FTId=PRO_1000064112. FT ACT_SITE 9 9 Tele-phosphohistidine intermediate (By FT similarity). FT ACT_SITE 182 182 By similarity. FT SITE 60 60 Interaction with carboxyl group of FT phosphoglycerates (By similarity). 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 //