ID   Q03KA9_STRTD            Unreviewed;       230 AA.
AC   Q03KA9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   10-JUL-2007, entry version 7.
DE   Phosphoglycerate mutase 1.
GN   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 + 2,3-diphosphoglycerate
CC       = 3-phospho-D-glycerate + 2,3-diphosphoglycerate.
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.
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   GenomeReviews; CP000419_GR; STER_1172.
DR   GO; GO:0016868; F:intramolecular transferase activity, phosph...; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
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.
KW   Complete proteome; Glycolysis; Isomerase.
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
//