ID   I0DID2_CORPS            Unreviewed;       248 AA.
AC   I0DID2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   03-APR-2013, entry version 9.
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=5.4.2.1;
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   EnsemblBacteria; AFH90100; AFH90100; Cp31_0266.
DR   GeneID; 12785813; -.
DR   KEGG; cop:Cp31_0266; -.
DR   KO; K01834; -.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA: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   Glycolysis; Isomerase.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    182    182       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (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
//