ID G0H949_BIFAN Unreviewed; 311 AA.
AC G0H949;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 03-APR-2013, entry version 10.
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=BALAC2494_00671;
OS Bifidobacterium animalis subsp. lactis CNCM I-2494.
OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1042403;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNCM I-2494;
RX PubMed=21914878; DOI=10.1128/JB.05716-11;
RA Chervaux C., Grimaldi C., Bolotin A., Quinquis B., Legrain-Raspaud S.,
RA van Hylckama Vlieg J.E., Denariaz G., Smokvina T.;
RT "Genome Sequence of the Probiotic Strain Bifidobacterium animalis
RT subsp. lactis CNCM I-2494.";
RL J. Bacteriol. 193:5560-5561(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNCM I-2494;
RA McNulty N.P.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002915; AEK29900.1; -; Genomic_DNA.
DR RefSeq; YP_005577619.1; NC_017215.1.
DR ProteinModelPortal; G0H949; -.
DR EnsemblBacteria; AEK29900; AEK29900; BALAC2494_00671.
DR GeneID; 12174410; -.
DR KEGG; bnm:BALAC2494_00671; -.
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 75 75 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 245 245 By similarity.
FT SITE 126 126 Interaction with carboxyl group of
FT phosphoglycerates (By similarity).
SQ SEQUENCE 311 AA; 34636 MW; C08F3C9B42814F81 CRC64;
MWPSGNTVAP CGICRGSRSP SRWCSSVSPC PSECAEIVAF ADYPANRADM AMHVHLTRRV
ARLGHMTYKL VLLRHGQSEW NKTNQFTGWV DVPLTEKGRE EAKNGGKLMK DKGVLPDIVF
TSLLRRAINT ANIALDEADR LWIPVKRDWR LNERHYGALQ GKNKTEIREE YGDEKFMLWR
RSYGTPPPEI DPNDQYAQNN DPRYAGDPVP EAECLADVVA RVEPYWEAEI IPELKSGKTV
LIAAHGNSLR AIVKMLDGLT EEEIAKVNIP TAIPLVYELD ENFKPIKKGG EYLDPEAAAA
GAAAVAAQGQ K
//
