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   13-SEP-2023, entry version 137.
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   EnsemblFungi; C2_05460W_A-T; C2_05460W_A-T-p1; C2_05460W_A.
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; RVHHIGE; -.
DR   OrthoDB; 312683at2759; -.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR   COMPLUYEAST-2DPAGE; P46614; -.
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
//