KPYK1_TRYBB
ID KPYK1_TRYBB Reviewed; 499 AA.
AC P30615;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pyruvate kinase 1;
DE Short=PK 1;
DE EC=2.7.1.40;
GN Name=PYK1;
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; X57950; CAA41018.1; -; Genomic_DNA.
DR PIR; S17648; S17648.
DR PDB; 4HYV; X-ray; 2.30 A; A/B=1-499.
DR PDB; 4HYW; X-ray; 2.35 A; A/B=1-499.
DR PDB; 4KCT; X-ray; 1.95 A; A/B=1-499.
DR PDB; 4KCU; X-ray; 2.35 A; A/B=1-499.
DR PDB; 4KCV; X-ray; 2.18 A; A/B=1-499.
DR PDB; 4KCW; X-ray; 2.50 A; A/B=1-499.
DR PDBsum; 4HYV; -.
DR PDBsum; 4HYW; -.
DR PDBsum; 4KCT; -.
DR PDBsum; 4KCU; -.
DR PDBsum; 4KCV; -.
DR PDBsum; 4KCW; -.
DR AlphaFoldDB; P30615; -.
DR SMR; P30615; -.
DR BRENDA; 2.7.1.40; 6520.
DR SABIO-RK; P30615; -.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate;
KW Transferase.
FT CHAIN 1..499
FT /note="Pyruvate kinase 1"
FT /id="PRO_0000112103"
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"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4HYV"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4KCT"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4KCT"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:4KCT"
FT TURN 228..233
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:4KCT"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:4KCT"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:4KCT"
SQ SEQUENCE 499 AA; 54467 MW; 1D40AD5352B272C6 CRC64;
MSQLEHNIGL SIFEPVAKHR ANRIVCTIGP STQSVEALKN LMKSGMSVAR MNFSHGSHEY
HQTTINNVRA AAAELGLHIG IALDTKGPEI RTGLFKDGEV SFAPGDIVCV TTDPAYEKVG
TKEKFYIDYP QLTNAVRPGG SIYVDDGVMT LRVVSKEDDR 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
