PGK_CANMA
ID PGK_CANMA Reviewed; 417 AA.
AC P41757;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK1;
OS Candida maltosa (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RX PubMed=8082186; DOI=10.1007/bf00351779;
RA Masuda Y., Park S.M., Ohkuma M., Ohta A., Takagi M.;
RT "Expression of an endogenous and a heterologous gene in Candida maltosa by
RT using a promoter of a newly-isolated phosphoglycerate kinase (PGK) gene.";
RL Curr. Genet. 25:412-417(1994).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; D12474; BAA02040.1; -; Genomic_DNA.
DR PIR; S43525; JT0950.
DR AlphaFoldDB; P41757; -.
DR SMR; P41757; -.
DR PRIDE; P41757; -.
DR UniPathway; UPA00109; UER00185.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..417
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145878"
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; 44947 MW; CA22E3D2F3D1D8F1 CRC64;
MSLSNKLSVK DLNVTGKRVF IRVDFNVPLD GKTITNNQRI VAALPTIKYV EEQKPKCIIL
ASHLGRPNGE RNEKYSLAPV AAELEKLLGQ KVTFLDDCVG PEVTKAVDSA TEGQIFLLEN
LRFHIEEEGS AKDKDGKKTK ADPEAVKKFR EQLTSLADVY VNDAFGTAHR AHSSMVGLEV
PERAAGFLMS KELEYFAKAL ENPQRPFLAI LGGAKVSDKI QLIDNLLDKV DMLIVGGGMA
FTFKKVLNNM PIGDSLFDEA GAKNVENLVA KAKKNNVELI LPVDFVTADK FDKDAEVSTA
DDVTGIPDKW MGLDCGPKSR KLFADAVAKA KTIVWNGPPG VFEFDKFAEG TKSLLDDAVK
SAEVGNIVII GGGDTATVAK KYGVVDKLSH VSTGGGASLE LLEGKELPGV TALSNKA