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Database: UniProt/SWISS-PROT
Entry: GPMA_STAES
LinkDB: GPMA_STAES
Original site: GPMA_STAES 
ID   GPMA_STAES              Reviewed;         228 AA.
AC   Q8CN61;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   10-OCT-2018, entry version 98.
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=SE_1995;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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}.
DR   EMBL; AE015929; AAO05636.1; -; Genomic_DNA.
DR   RefSeq; NP_765550.1; NC_004461.1.
DR   RefSeq; WP_001831569.1; NC_004461.1.
DR   ProteinModelPortal; Q8CN61; -.
DR   SMR; Q8CN61; -.
DR   STRING; 176280.SE1995; -.
DR   PRIDE; Q8CN61; -.
DR   EnsemblBacteria; AAO05636; AAO05636; SE_1995.
DR   GeneID; 1057821; -.
DR   KEGG; sep:SE1995; -.
DR   PATRIC; fig|176280.10.peg.1949; -.
DR   eggNOG; ENOG4105DKJ; Bacteria.
DR   eggNOG; COG0588; LUCA.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   BioCyc; SEPI176280:G1G05-2054-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    228       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000179916.
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   228 AA;  26755 MW;  AF122ACBF2FFB0DE CRC64;
     MPKLILCRHG QSEWNAKNLF TGWADVKLSK QGIEEAQSAG KKIYDNQIEI DIAFTSLLTR
     ALETTQYILA GSDQQWIPVY KSWRLNERHY GGLQGLNKDD ARKKWGEDQV HQWRRSYDVR
     PPRESEEQRE AYLKNRRYQH IDHRMMPYCE SLKDTLERVV PFWTDHISQH LLDDKTVLVS
     AHGNSIRALI KYLEGLSEED IVGYEIKTGA PLVYELTDDL VVKDKYYL
//
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