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-MAR-2010, entry version 26.
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.
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DR   EMBL; CP000419; ABJ66363.1; -; Genomic_DNA.
DR   RefSeq; YP_820559.1; -.
DR   SMR; Q03KA9; 1-229.
DR   STRING; Q03KA9; -.
DR   GeneID; 4438655; -.
DR   GenomeReviews; CP000419_GR; STER_1172.
DR   KEGG; ste:STER_1172; -.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HBG658938; -.
DR   OMA; VPLTECL; -.
DR   ProtClustDB; PRK14117; -.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphogl...; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_01039; PGAM_GpmA; 1; -.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 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   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
//