ID E3D976_GARV3 Unreviewed; 246 AA.
AC E3D976;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 01-MAY-2013, entry version 16.
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; OrderedLocusNames=HMPREF0421_20538;
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317;
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M.,
RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X.,
RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K.,
RA Nelson K.E., Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals
RT substantial differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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; CP002104; ADP38620.1; -; Genomic_DNA.
DR RefSeq; YP_003985643.1; NC_014644.1.
DR ProteinModelPortal; E3D976; -.
DR EnsemblBacteria; ADP38620; ADP38620; HMPREF0421_20538.
DR GeneID; 9904092; -.
DR KEGG; gvg:HMPREF0421_20538; -.
DR PATRIC; 42627947; VBIGarVag39333_0536.
DR HOGENOM; HOG000221682; -.
DR KO; K01834; -.
DR BioCyc; GVAG525284:GI3V-559-MONOMER; -.
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 Complete proteome; Glycolysis; Isomerase.
FT ACT_SITE 10 10 Tele-phosphohistidine intermediate (By
FT similarity).
FT ACT_SITE 180 180 By similarity.
FT SITE 61 61 Interaction with carboxyl group of
FT phosphoglycerates (By similarity).
SQ SEQUENCE 246 AA; 27713 MW; EA0BB88C4943DED9 CRC64;
MTYKLVLLRH GQSAWNKTNQ FTGWVDVPLT EQGVEEAKHG GELLKEKNVL PDIVFTSLLR
RAINTANYAL DAADRLWIPV RRSWRLNERH YGALQGKNKS EIRQEYGDEK FMIWRRSYAT
PPPEIDPNDE YSQTNDPRYA GDPVPETEAL ANVVTRVTPY WESDIIPELK SGKTVMIAAH
GNSLRAIVKM LDNLSEEEIS KVNIPTAIPL LYELDENFKP IKPRGEYLDP EAAAAGAAAV
AAQGQK
//
