PGK_CANAL
ID PGK_CANAL Reviewed; 417 AA.
AC P46273; A0A1D8PPF5; Q59NN7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK1; OrderedLocusNames=CAALFM_C600750CA;
GN ORFNames=CaO19.11135, CaO19.3651;
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 [GENOMIC DNA].
RC STRAIN=3153A;
RX PubMed=9043109; DOI=10.1099/00221287-143-2-321;
RA Alloush H.M., Lopez-Ribot J.L., Masten B.J., Chaffin W.L.;
RT "3-phosphoglycerate kinase: a glycolytic enzyme protein present in the cell
RT wall of Candida albicans.";
RL Microbiology 143:321-330(1997).
RN [2]
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 [3]
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 [4]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; U25180; AAA66523.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30021.1; -; Genomic_DNA.
DR RefSeq; XP_711323.1; XM_706231.2.
DR AlphaFoldDB; P46273; -.
DR SMR; P46273; -.
DR BioGRID; 1230131; 2.
DR STRING; 237561.P46273; -.
DR Allergome; 5991; Cand a PGK.
DR MoonProt; P46273; -.
DR COMPLUYEAST-2DPAGE; P46273; -.
DR PRIDE; P46273; -.
DR GeneID; 3647081; -.
DR KEGG; cal:CAALFM_C600750CA; -.
DR CGD; CAL0000184891; PGK1.
DR VEuPathDB; FungiDB:C6_00750C_A; -.
DR HOGENOM; CLU_025427_0_2_1; -.
DR InParanoid; P46273; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR BRENDA; 2.7.2.3; 1096.
DR UniPathway; UPA00109; UER00185.
DR PRO; PR:P46273; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0051701; P:biological process involved in interaction with host; IPI:CGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell wall; Cell wall biogenesis/degradation; Cytoplasm;
KW Glycolysis; Kinase; Nucleotide-binding; Reference proteome; Secreted;
KW Transferase.
FT CHAIN 1..417
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145876"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 45180 MW; 6F147F640F5EC784 CRC64;
MSLSNKLSVK DLDVAGKRVF IRVDFNVPLD GKTITNNQRI VAALPTIKYV EEHKPKYIVL
ASHLGRPNGE RNDKYSLAPV ATELEKLLGQ KVTFLNDCVG PEVTKAVENA KDGEIFLLEN
LRYHIEEEGS SKDKDGKKVK ADPEAVKKFR QELTSLADVY INDAFGTAHR AHSSMVGLEV
PQRAAGFLMS KELEYFAKAL ENPERPFLAI LGGAKVSDKI QLIDNLLDKV DMLIVGGGMA
FTFKKILNKM PIGDSLFDEA GAKNVEHLVE KAKKNNVELI LPVDFVTADK FDKDAKTSSA
TDAEGIPDNW MGLDCGPKSV ELFQQAVAKA KTIVWNGPPG VFEFEKFANG TKSLLDAAVK
SAENGNIVII GGGDTATVAK KYGVVEKLSH VSTGGGASLE LLEGKDLPGV VALSNKN
