KPYK_CANAL
ID KPYK_CANAL Reviewed; 504 AA.
AC P46614; A0A1D8PHF3; Q59ZE4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=CDC19; Synonyms=PYK1; OrderedLocusNames=CAALFM_C205460WA;
GN ORFNames=CaO19.11059, CaO19.3575;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-181.
RX PubMed=8406815; DOI=10.1128/iai.61.10.4263-4271.1993;
RA Swoboda R.K., Bertram G., Hollander H., Greenspan D., Greenspan J.S.,
RA Gow N.A., Gooday G.W., Brown A.J.;
RT "Glycolytic enzymes of Candida albicans are nonubiquitous immunogens during
RT candidiasis.";
RL Infect. Immun. 61:4263-4271(1993).
RN [5]
RP PROTEIN SEQUENCE OF 221-229 AND 404-409, AND IDENTIFICATION BY MASS
RP 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 404-409, 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=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=S65775; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP017624; AOW27559.1; -; Genomic_DNA.
DR EMBL; S65775; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_714934.1; XM_709841.1.
DR AlphaFoldDB; P46614; -.
DR SMR; P46614; -.
DR BioGRID; 1226503; 6.
DR STRING; 237561.P46614; -.
DR COMPLUYEAST-2DPAGE; P46614; -.
DR PRIDE; P46614; -.
DR GeneID; 3643438; -.
DR KEGG; cal:CAALFM_C205460WA; -.
DR CGD; CAL0000192883; CDC19.
DR VEuPathDB; FungiDB:C2_05460W_A; -.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P46614; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 933620at2759; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:P46614; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; ISS:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006096; P:glycolytic process; ISS:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..504
FT /note="Pyruvate kinase"
FT /id="PRO_0000112109"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 55
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 244
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="I -> T (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="T -> H (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="P -> T (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Y -> I (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> Q (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="K -> M (in Ref. 4; S65775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55445 MW; 38518DDA54735113 CRC64;
MSHSSLSWLS NFNVETVPSK YLRRSSIIGT IGPKTNNVDV LVKLRKAGLN VVRMNFSHGS
YEYHQSVIDN ARKSEEVYKG RPLAIALDTK GPEIRTGTTI GDKDYPIPPN HEMIFTTDDA
YKTKCDDKVM YIDYKNITKV IAPGKIIYVD DGVLSFEVIS VDDEQTLKVR SLNAGKISSH
KGVNLPGTDV DLPALSEKDI ADIKFGVKNK VHMIFASFIR TANDVLEIRK VLGEEGKDIQ
IISKIENQQG VNNFDEILEV TDGVMVARGD LGIEIPAPQV FVVQKQLIAK CNLAAKPVIC
ATQMLESMTY NPRPTRAEVS DVGNAILDGA DCVMLSGETA KGNYPVEAVS MMHNTCLTAE
KAIAYPQLFN ELRSLAKKPT ATTETCAVAA VSAAYEQDAK AIVVLSTSGL SARLVSKYKP
DVPILMVTRN ERAAKFSHLY RGVYPFIYDK PSIENWQEDV ENRLRWAVSE AVELGIISKG
DSIVTVQGWT RGSGHSNTVR IVQA
