KPYK_YARLI
ID KPYK_YARLI Reviewed; 515 AA.
AC P30614; Q6C2B7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=PYK1; OrderedLocusNames=YALI0F09185g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 8662 / IFO 1209 / NRRL Y-1094;
RX PubMed=1511886; DOI=10.1016/0378-1119(92)90249-o;
RA Strick C.A., James L.C., O'Donnell M.M., Gollaher M.G., Franke A.E.;
RT "The isolation and characterization of the pyruvate kinase-encoding gene
RT from the yeast Yarrowia lipolytica.";
RL Gene 118:65-72(1992).
RN [2]
RP ERRATUM OF PUBMED:1511886.
RX PubMed=8125333; DOI=10.1016/0378-1119(94)90746-3;
RA Strick C.A., James L.C., O'Donnell M.M., Gollaher M.G., Franke A.E.;
RL Gene 140:141-143(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(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;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18520.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M86863; AAA18520.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; CR382132; CAG78002.2; -; Genomic_DNA.
DR PIR; JC1267; JC1267.
DR RefSeq; XP_505195.2; XM_505195.2.
DR AlphaFoldDB; P30614; -.
DR SMR; P30614; -.
DR STRING; 4952.CAG78002; -.
DR PRIDE; P30614; -.
DR EnsemblFungi; CAG78002; CAG78002; YALI0_F09185g.
DR GeneID; 2907873; -.
DR KEGG; yli:YALI0F09185g; -.
DR VEuPathDB; FungiDB:YALI0_F09185g; -.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P30614; -.
DR OMA; FERCDES; -.
DR BRENDA; 2.7.1.40; 1122.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..515
FT /note="Pyruvate kinase"
FT /id="PRO_0000112120"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 62
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 251
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 84..86
FT /note="QFQ -> RFR (in Ref. 1; AAA18520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56668 MW; ED3E51220306F1D6 CRC64;
MIYTANSSPS TNLQWLSTLN TDDIPTKNYR KSSIIGTIGP NTNSAEMISK LRQAGLNIVR
MNFSHGSYEY HQSVIENARE SEQQFQGRPL AIALDTKGPE IRTGVTKDDK DWDVKAGHVM
LFSTNPKYKD QCDDKIMYID YTNIVKQIDI GKIIFVDDGV LSFKVLEKID GETLKVETLN
NGKISSRKGV NLPGTDVDLP ALSEKDKADL KFGVEHGVDM IFASFVRTAN DVQAIRDVLG
EKGKGIQVIS KIENQQGVNN FDEILKETDG VMVARGDLGI EIPAPQVFIA QKQLIAKCNL
AGKPVICATQ MLDSMTYNPR PTRAEVSDVG NAVLDGADCV MLSGETAKGT YPIESVKMMH
ETCLVAEKAI AYAPLFNEMR TLTVRPTETV ETIAISAVSA SFEQQARAII VLSTSGTSAR
LCSKYRPNCP ILMVTRNAQA ARFSHLYRGV YPFIYHKARA SNPAEWQHDV EERLKWGMDE
AVALGILNKG DVVVAIQGWT GGLGHTNTLR VLECV
