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Database: UniProt/TrEMBL
Entry: I0DID2_CORPS
LinkDB: I0DID2_CORPS
Original site: I0DID2_CORPS 
ID   I0DID2_CORPS            Unreviewed;       248 AA.
AC   I0DID2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   19-FEB-2014, entry version 14.
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; ORFNames=Cp31_0266;
OS   Corynebacterium pseudotuberculosis 31.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1087451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=31;
RX   PubMed=23144408; DOI=10.1128/JB.01782-12;
RA   Silva A., Ramos R.T., Ribeiro Carneiro A., Cybelle Pinto A.,
RA   de Castro Soares S., Rodrigues Santos A., Silva Almeida S.,
RA   Guimaraes L.C., Figueira Aburjaile F., Vieira Barbosa E.G.,
RA   Alves Dorella F., Souza Rocha F., Souza Lopes T., Kawasaki R.,
RA   Gomes Sa P., da Rocha Coimbra N.A., Teixeira Cerdeira L.,
RA   Silvanira Barbosa M., Cruz Schneider M.P., Miyoshi A., Selim S.A.,
RA   Moawad M.S., Azevedo V.;
RT   "Complete Genome Sequence of Corynebacterium pseudotuberculosis Cp31,
RT   Isolated from an Egyptian Buffalo.";
RL   J. Bacteriol. 194:6663-6664(2012).
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.
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DR   EMBL; CP003421; AFH90100.1; -; Genomic_DNA.
DR   RefSeq; YP_006212790.1; NC_017730.1.
DR   ProteinModelPortal; I0DID2; -.
DR   EnsemblBacteria; AFH90100; AFH90100; Cp31_0266.
DR   GeneID; 12785813; -.
DR   KEGG; cop:Cp31_0266; -.
DR   KO; K01834; -.
DR   BioCyc; CPSE1087451:GLBU-278-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:glycolysis; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
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   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   REGION       23     24       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION       89     92       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   REGION      116    117       2-phospho-D-glycerate binding (By
FT                                similarity).
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    182    182       By similarity.
FT   BINDING      17     17       2-phospho-D-glycerate (By similarity).
FT   BINDING      62     62       2-phospho-D-glycerate (By similarity).
FT   BINDING     100    100       2-phospho-D-glycerate (By similarity).
FT   BINDING     184    184       2-phospho-D-glycerate (By similarity).
SQ   SEQUENCE   248 AA;  27537 MW;  027A1049EF9F070D CRC64;
     MTIGKLILLR HGQSEWNASN QFTGWVDVNL TEQGEAEAKR GGEMLKQQDV LPTVVYTSLL
     RRAIRTANIA LNAADRHWIP VVRDWRLNER HYGALQGLNK AETKDKYGAD QFMEWRRSYG
     TPPPELEDSS EFSQANDPRY ADLSQVPRME CLKDVVERFV PYFEEEILPR AKKGETVLIA
     AHGNSLRALV KHLDNISDAD IAELNIPTGI PLVYELDQEG KVLNPGGTYL DPEAAAAGAA
     AVAAQGGK
//
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