ID   KPYK2_TRYBB             Reviewed;         499 AA.
AC   P30616;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Pyruvate kinase 2;
DE            Short=PK 2;
DE            EC=2.7.1.40;
GN   Name=PYK2;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=427;
RX   PubMed=1879424; DOI=10.1111/j.1432-1033.1991.tb21043.x;
RA   Allert S., Ernest I., Poliszczak A., Opperdoes F.R., Michels P.A.M.;
RT   "Molecular cloning and analysis of two tandemly linked genes for pyruvate
RT   kinase of Trypanosoma brucei.";
RL   Eur. J. Biochem. 200:19-27(1991).
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   -!- ACTIVITY REGULATION: Activated by fructose 2,6-bisphosphate, activated
CC       by the effector in a cooperative manner.
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}.
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DR   EMBL; X57951; CAA41019.1; -; Genomic_DNA.
DR   PIR; S17649; S17649.
DR   AlphaFoldDB; P30616; -.
DR   SMR; P30616; -.
DR   SABIO-RK; P30616; -.
DR   UniPathway; UPA00109; UER00188.
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; IEA:UniProtKB-EC.
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   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT   CHAIN           1..499
FT                   /note="Pyruvate kinase 2"
FT                   /id="PRO_0000112104"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         52
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            239
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  54452 MW;  7FE8238E73E45CA2 CRC64;
     MSQLEHNIGL SIFEPVAKHR ANRIVCTIGP STQSVEALKN LMKSGMSVAR MNFSHGSHEY
     HQTTINNVRA AAAELGLHIG IALDTKGPEI RTGLFKDGEV TFAPGDIVCV TTDPAYEKVG
     TKEKFYIDYP QLTKAVPVGG SIYVDDGVMT LRVLSKEDDR TLKCHVNNHH RLTDRRGINL
     PGCEVDLPAV SEKDRKDLEF GVAQGVDMIF ASFIRTAEQV REVRAALGEK GKDILIISKI
     ENHQGVQNID SIIEASNGIM VARGDLGVEI PAEKVCVAQM CIISKCNVVG KPVICATQML
     ESMTSNPRPT RAEVSDVANA VLNGADCVML SGETAKGKYP NEVVQYMARI CVEAQSATHD
     TVMFNSIKNL QKIPMCPEEA VCSSAVASAF EVQAKAMLVL SNTGRSARLI SKYRPNCPII
     CVTTRLQTCR QLNVTRSVVS VFYDAAKSGE DKDKEKRVKL GLDFAKKEKY ASTGDVVVVV
     HADHSVKGYP NQTRLIYLP