PMGY_CANAL
ID PMGY_CANAL Reviewed; 248 AA.
AC P82612; A0A1D8PGZ2; Q5AH93;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphoglycerate mutase;
DE Short=PGAM;
DE EC=5.4.2.11;
DE AltName: Full=BPG-dependent PGAM;
DE AltName: Full=MPGM;
DE AltName: Full=Phosphoglyceromutase;
GN Name=GPM1; OrderedLocusNames=CAALFM_C203270WA;
GN ORFNames=CaO19.8522, CaO19.903;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Pitarch A., Diaz-Orejas R., Molero G., Pardo M., Sanchez M., Nombela C.,
RA Gil C.;
RT "A proteomic approach to analyse the serologic response to Candida albicans
RT systemic infection in a murine model.";
RL Submitted (JUN-2000) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 61-77, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10949142;
RX DOI=10.1002/1522-2683(20000701)21:13<2651::aid-elps2651>3.0.co;2-3;
RA Pardo M., Ward M., Pitarch A., Sanchez M., Nombela C., Blackstock W.,
RA Gil C.;
RT "Cross-species identification of novel Candida albicans immunogenic
RT proteins by combination of two-dimensional polyacrylamide gel
RT electrophoresis and mass spectrometry.";
RL Electrophoresis 21:2651-2659(2000).
RN [6]
RP PROTEIN SEQUENCE OF 99-109, SUBCELLULAR LOCATION, AND ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(2004).
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;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; CP017624; AOW27363.1; -; Genomic_DNA.
DR RefSeq; XP_721022.1; XM_715929.2.
DR AlphaFoldDB; P82612; -.
DR SMR; P82612; -.
DR BioGRID; 1220370; 5.
DR STRING; 237561.P82612; -.
DR MoonProt; P82612; -.
DR COMPLUYEAST-2DPAGE; P82612; -.
DR PRIDE; P82612; -.
DR GeneID; 3637431; -.
DR KEGG; cal:CAALFM_C203270WA; -.
DR CGD; CAL0000185566; GPM1.
DR VEuPathDB; FungiDB:C2_03270W_A; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P82612; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 804949at2759; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:P82612; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; NAS:CGD.
DR GO; GO:0051701; P:biological process involved in interaction with host; IPI:CGD.
DR GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 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 PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Isomerase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..248
FT /note="Phosphoglycerate mutase"
FT /id="PRO_0000179837"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT CONFLICT 62..63
FT /note="IQ -> LK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27454 MW; 5CC0282E8EFCC6A2 CRC64;
MPKLVLVRHG QSEWNEKNLF TGWVDVRLSE TGQKEAKRAG ELLKEAGINV DVLHTSKLSR
AIQTANIALD AADQLYVPVK RSWRLNERHY GALQGKDKAQ TLEAYGQEKF QIWRRSFDVP
PPKIDPKDEY SQVGDRRYAD VDPAVVPLTE SLALVIDRLL PYWQDEIAGD LLAGKVVLIA
AHGNSLRALV KHLDNISDED IAGLNIPTGI PLVYELDENL KPTKPSYYLD PEAAAAGAAA
VAAQGQKK
