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Database: UniProt
Entry: P65708
LinkDB: P65708
Original site: P65708 
ID   GPMA_STAAM              Reviewed;         228 AA.
AC   P65708; Q99RL4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   22-JUL-2015, entry version 69.
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=SAV2416;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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}.
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DR   EMBL; BA000017; BAB58578.1; -; Genomic_DNA.
DR   RefSeq; WP_001125208.1; NC_002758.2.
DR   ProteinModelPortal; P65708; -.
DR   SMR; P65708; 1-228.
DR   STRING; 158878.SAV2416; -.
DR   World-2DPAGE; 0002:P65708; -.
DR   EnsemblBacteria; BAB58578; BAB58578; SAV2416.
DR   GeneID; 23198223; -.
DR   KEGG; sav:SAV2416; -.
DR   PATRIC; 19565750; VBIStaAur52173_2501.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; PIKRYYL; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   PhylomeDB; P65708; -.
DR   BioCyc; SAUR158878:GJJ5-2484-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
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_0000179911.
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    182    182       {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}.
SQ   SEQUENCE   228 AA;  26680 MW;  1751F3AFB1EE068E CRC64;
     MPKLILCRHG QSEWNAKNLF TGWEDVNLSE QGINEATRAG EKVRENNIAI DVAFTSLLTR
     ALDTTHYILT ESKQQWIPVY KSWRLNERHY GGLQGLNKDD ARKEFGEEQV HIWRRSYDVK
     PPAETEEQRE AYLADRRYNH LDKRMMPYSE SLKDTLVRVI PFWTDHISQY LLDGQTVLVS
     AHGNSIRALI KYLEDVSDED IINYEIKTGA PLVYELTDDL EVIDKYYL
//
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