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Database: UniProt/TrEMBL
Entry: B9WB10_CANDC
LinkDB: B9WB10_CANDC
Original site: B9WB10_CANDC 
ID   B9WB10_CANDC            Unreviewed;       248 AA.
AC   B9WB10;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
GN   OrderedLocusNames=Cd36_18020 {ECO:0000313|CGD:CAL0000159680};
GN   ORFNames=CD36_18020 {ECO:0000313|EMBL:CAX43580.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX43580.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX43580.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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|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}.
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DR   EMBL; FM992689; CAX43580.1; -; Genomic_DNA.
DR   RefSeq; XP_002418280.1; XM_002418235.1.
DR   AlphaFoldDB; B9WB10; -.
DR   GeneID; 8045838; -.
DR   KEGG; cdu:CD36_18020; -.
DR   CGD; CAL0000159680; Cd36_18020.
DR   VEuPathDB; FungiDB:CD36_18020; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   HOGENOM; CLU_033323_1_1_1; -.
DR   OrthoDB; 1008469at2759; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002605; Chromosome 2.
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; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 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}.
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        87
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         8..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         21..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         87..90
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         114..115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         183..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            182
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   248 AA;  27470 MW;  160B56F0CA886145 CRC64;
     MPKLVLVRHG QSEWNEKNLF TGWVDVRLSE TGQKEAKRAG ELLKEAGIKV DVLHTSKLSR
     AIQTANIALD AADQLYVPVK RSWRLNERHY GALQGKDKAQ TLETYGQEKF QIWRRSFDVP
     PPTIDPKDQY SQVGDRRYAD IDPAVVPLTE SLALVIDRLL PYWQDEIAGD LLAGKVVLIA
     AHGNSLRGLV KHLDNISDED IAGLNIPTGI PLVYELDENL KPTKPSYYLD PEAAAAGAAA
     VAAQGQKK
//
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