GenomeNet

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   09-JUL-2014, entry version 62.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE            Short=BPG-dependent PGAM;
DE            Short=PGAM;
DE            Short=Phosphoglyceromutase;
DE            Short=dPGM;
DE            EC=5.4.2.11;
GN   Name=gpmA; 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 (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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000017; BAB58578.1; -; Genomic_DNA.
DR   RefSeq; NP_372940.1; 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; 1122441; -.
DR   KEGG; sav:SAV2416; -.
DR   PATRIC; 19565750; VBIStaAur52173_2501.
DR   eggNOG; COG0588; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; KDDERFP; -.
DR   OrthoDB; EOG6C8N1H; -.
DR   PhylomeDB; P65708; -.
DR   BioCyc; SAUR158878:GJJ5-2484-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP.
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   1: Evidence at protein level;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    228       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000179911.
FT   REGION       21     22       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION       87     90       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION      114    115       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   ACT_SITE      9      9       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    182    182       By similarity.
FT   BINDING      15     15       2-phospho-D-glycerate (By similarity).
FT   BINDING      60     60       2-phospho-D-glycerate (By similarity).
FT   BINDING      98     98       2-phospho-D-glycerate (By similarity).
FT   BINDING     184    184       2-phospho-D-glycerate (By similarity).
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
//
DBGET integrated database retrieval system