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   16-OCT-2013, entry version 51.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE            Short=BPG-dependent PGAM;
DE            Short=PGAM;
DE            Short=Phosphoglyceromutase;
DE            Short=dPGM;
DE            EC=5.4.2.11;
GN   Name=gpmA; 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 (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.
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DR   EMBL; CP000419; ABJ66363.1; -; Genomic_DNA.
DR   RefSeq; YP_820559.1; NC_008532.1.
DR   ProteinModelPortal; Q03KA9; -.
DR   SMR; Q03KA9; 1-229.
DR   STRING; 322159.STER_1172; -.
DR   EnsemblBacteria; ABJ66363; ABJ66363; STER_1172.
DR   GeneID; 4438655; -.
DR   KEGG; ste:STER_1172; -.
DR   PATRIC; 19799690; VBIStrThe129203_1196.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; SYYLGDQ; -.
DR   ProtClustDB; PRK14117; -.
DR   BioCyc; STHE322159:GJ9F-1172-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01039; PGAM_GpmA; 1; -.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; 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   REGION       21     22       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION       87     90       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION      114    115       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   ACT_SITE      9      9       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    182    182       By similarity.
FT   BINDING      15     15       2-phospho-D-glycerate (By similarity).
FT   BINDING      60     60       2-phospho-D-glycerate (By similarity).
FT   BINDING      98     98       2-phospho-D-glycerate (By similarity).
FT   BINDING     184    184       2-phospho-D-glycerate (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
//