ID A0A4V3WL35_CAMSI Unreviewed; 291 AA.
AC A0A4V3WL35;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=TEA_003569 {ECO:0000313|EMBL:THG03187.1};
OS Camellia sinensis var. sinensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=542762 {ECO:0000313|EMBL:THG03187.1, ECO:0000313|Proteomes:UP000306102};
RN [1] {ECO:0000313|EMBL:THG03187.1, ECO:0000313|Proteomes:UP000306102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shuchazao {ECO:0000313|Proteomes:UP000306102};
RC TISSUE=Leaf {ECO:0000313|EMBL:THG03187.1};
RX PubMed=29678829; DOI=.1073/pnas.1719622115;
RA Wei C., Yang H., Wang S., Zhao J., Liu C., Gao L., Xia E., Lu Y., Tai Y.,
RA She G., Sun J., Cao H., Tong W., Gao Q., Li Y., Deng W., Jiang X., Wang W.,
RA Chen Q., Zhang S., Li H., Wu J., Wang P., Li P., Shi C., Zheng F., Jian J.,
RA Huang B., Shan D., Shi M., Fang C., Yue Y., Li F., Li D., Wei S., Han B.,
RA Jiang C., Yin Y., Xia T., Zhang Z., Bennetzen J.L., Zhao S., Wan X.;
RT "Draft genome sequence of Camellia sinensis var. sinensis provides insights
RT into the evolution of the tea genome and tea quality.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E4151-E4158(2018).
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; Evidence={ECO:0000256|ARBA:ARBA00001174,
CC ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THG03187.1}.
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DR EMBL; SDRB02011023; THG03187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3WL35; -.
DR STRING; 542762.A0A4V3WL35; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000306102; Unassembled WGS sequence.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF21; 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; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000306102};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 1..134
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 173..272
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 291 AA; 32078 MW; F5753627F60896A2 CRC64;
MSFVNDADAV NHLKNHLSTK TSASIKVLAK IESMESLHKL EEIVEASDGI MVARGDLGVE
IPLEQIPTVQ ETITHVCRQL NKPVIVASQL LESMIEYPTP TRAEVADVSE AVRQFADALM
LSGESAIGSY GQKALSVLRT TSSRMELWSR EENRQNGLYQ RQLGQSLPDR IAEQICNCAV
EMANNLGLDA IFVYTKRGHM ASLFSRNRPN PPIFAFTNNE STRMALTLQW GVMPVLVDLS
DDIEVNISKT VDLMKTKGMV EEGDAVLVVS DVIPSCETPT VFQSIQVKTI V
//
