KPYC_TOBAC
ID KPYC_TOBAC Reviewed; 508 AA.
AC Q42954;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Pyruvate kinase, cytosolic isozyme;
DE Short=PK;
DE EC=2.7.1.40;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7865798; DOI=10.1007/bf00019180;
RA Blakeley S.D., Gottlob-Mchugh S., Wan J., Crews L., Miki B., Ko K.,
RA Dennis D.T.;
RT "Molecular characterization of plastid pyruvate kinase from castor and
RT tobacco.";
RL Plant Mol. Biol. 27:79-89(1995).
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.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; Z29492; CAA82628.1; -; mRNA.
DR PIR; S41379; S41379.
DR RefSeq; NP_001312569.1; NM_001325640.1.
DR AlphaFoldDB; Q42954; -.
DR SMR; Q42954; -.
DR STRING; 4097.Q42954; -.
DR GeneID; 107797877; -.
DR KEGG; nta:107797877; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000084051; Unplaced.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..508
FT /note="Pyruvate kinase, cytosolic isozyme"
FT /id="PRO_0000112127"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 50
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 55133 MW; A8FC5DA9D7CB9989 CRC64;
MAIENNNNGV NFCTVKRPKT KIVCTLGPAS RSVPMIEKLL RAGMNVARFN FSHGSHDYHQ
ETIDNLRQAM ESTGILCAVM LDTKGPEIRT GFLKDAKPVQ LKQGQEITIS TDYSIKGDES
MICMSYKKLA EDVKPQSVIL CADGQITFTV LSCDKENGLD RCRCENTAVL GERKNVNLPG
VIVDLPTLTD KDKDDILNWG VPNHIDMIAL SFVRKGSDLV EVRKLLGEHA KNILLMSKVE
NQEGVANFDD ILLNSDAFMV ARGDLGMEIP IEKIFLAQKV MIYKCNIQGK PVVTATQMLE
SMIKSPRPTR AEATDVANAV LDGTDCVMLS GETAAGAYPD LAVGTMAKIC IEAESTIDYP
DVFKRIMSNA PVPMSPLESL ASSAVRTANS AKAALILVLT RGGSTAKLVA KYRPGMPILS
VVVPEIKTDS FDWTCSDESP ARHSLIFRGL VPVLHAGSAR ASHEESTEEA LDFALQHAKT
KGLCKQGDSV VALHRVGTAS VIKIVTVK
