ID I2JSW8_DEKBR Unreviewed; 284 AA.
AC I2JSW8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
GN ORFNames=AWRI1499_4036 {ECO:0000313|EMBL:EIF46070.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF46070.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF46070.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF46070.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380,
CC ECO:0000256|RuleBase:RU004511};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798,
CC ECO:0000256|RuleBase:RU004511}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|RuleBase:RU004511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIF46070.1}.
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DR EMBL; AHIQ01000229; EIF46070.1; -; Genomic_DNA.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000004997; Unassembled WGS sequence.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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 NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511};
KW Reference proteome {ECO:0000313|Proteomes:UP000004997}.
FT ACT_SITE 45
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 125
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 44..51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 125..128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 152..153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 228
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 284 AA; 32297 MW; 72D25DB427012F12 CRC64;
MVRSGFHLIV HILTTQGSST SDYXIVIIES RSNILEMPHL IVLRHGESEW NKTNKFCGWV
DVSLSENGKK QAERSAELLL KQKEVGKPDI CFTSRLTRAN QTAEIILDRM HRLFIDTDKT
WRLNERHYGA FQXRDKTEVL AEVGKEKYMF VRRAYTGCPP LCDPDAECRS LDDRYNLDAE
DEKKLGLSGG EMPRGESLEM VVGRLVPYYK AAIEPELAKG RTVLVVTHGS VVRALLKVLY
SISDDDISEV NIPNGIPIKI DLDAETLKPR KDKWEYLDPE RGQG
//
