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Database: UniProt/SWISS-PROT
Entry: GPMA_STAEQ
LinkDB: GPMA_STAEQ
Original site: GPMA_STAEQ 
ID   GPMA_STAEQ              Reviewed;         228 AA.
AC   Q5HLI0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=SERP2007;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phospho-D-glycerate = 3-phospho-D-glycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.11; Evidence={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; CP000029; AAW52808.1; -; Genomic_DNA.
DR   RefSeq; WP_002438282.1; NC_002976.3.
DR   ProteinModelPortal; Q5HLI0; -.
DR   SMR; Q5HLI0; -.
DR   STRING; 176279.SERP2007; -.
DR   PRIDE; Q5HLI0; -.
DR   EnsemblBacteria; AAW52808; AAW52808; SERP2007.
DR   KEGG; ser:SERP2007; -.
DR   eggNOG; ENOG4105DKJ; Bacteria.
DR   eggNOG; COG0588; LUCA.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   BioCyc; SEPI176279:G1G46-2068-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000531; 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;
KW   Reference proteome.
FT   CHAIN         1    228       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000179917.
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;  26697 MW;  CC13F81A21FFB3DF CRC64;
     MPKLILCRHG QSEWNAKNLF TGWADVKLSK QGIEEAQSAG KKIYGNQIEI DIAFTSLLTR
     ALETTQYILA GSDQQWIPVY KSWRLNERHY GGLQGLNKDD ARKKWGEDQV HQWRRSYDVR
     PPRESEEQRE AYLKNRRYQH IDHRMMPYCE SLKDTLERVV PFWTDHISQH LLDDKTVLVS
     AHGNSIRALI KYLEGLSEED IVGYEIKTGA PLVYELTDDL VVKDKYYL
//
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