ID A0A6A6KQT6_HEVBR Unreviewed; 495 AA.
AC A0A6A6KQT6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=GH714_038679 {ECO:0000313|EMBL:KAF2289799.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:KAF2289799.1, ECO:0000313|Proteomes:UP000467840};
RN [1] {ECO:0000313|EMBL:KAF2289799.1, ECO:0000313|Proteomes:UP000467840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GT1 {ECO:0000313|Proteomes:UP000467840};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2289799.1};
RX PubMed=31838037; DOI=10.1016/j.molp.2019.10.017;
RA Liu J., Shi C., Shi C.C., Li W., Zhang Q.J., Zhang Y., Li K., Lu H.F.,
RA Shi C., Zhu S.T., Xiao Z.Y., Nan H., Yue Y., Zhu X.G., Wu Y., Hong X.N.,
RA Fan G.Y., Tong Y., Zhang D., Mao C.L., Liu Y.L., Hao S.J., Liu W.Q.,
RA Lv M.Q., Zhang H.B., Liu Y., Hu-Tang G.R., Wang J.P., Wang J.H., Sun Y.H.,
RA Ni S.B., Chen W.B., Zhang X.C., Jiao Y.N., Eichler E.E., Li G.H., Liu X.,
RA Gao L.Z.;
RT "The Chromosome-Based Rubber Tree Genome Provides New Insights into Spurge
RT Genome Evolution and Rubber Biosynthesis.";
RL Mol. Plant 13:336-350(2020).
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:KAF2289799.1}.
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DR EMBL; JAAGAX010000016; KAF2289799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A6KQT6; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000467840; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 2.40.33.10; PK beta-barrel domain-like; 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; IPR011037; Pyrv_Knase-like_insert_dom_sf.
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 NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF4; 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; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 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:UP000467840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 30..360
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 368..483
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 495 AA; 53739 MW; C8A59A755A343FB1 CRC64;
MHASHLLLEE PIRMASILEP SKASFFPAMT KIVGTLGPKS RSVEVISGCL KAGMSVARFD
FSWGDSEYHQ ETLENLKAAV KNTKKLCAVM LDTVGPELQV VNKSEKSISL LADGLVVLTP
NQEKEASSEV LPINFDGLSK AVKPGDTIFV GQYLFTGSET TSVWLEVSEV KDSDVICVIK
NSATLAGSLF TLHASQIRID LPTLSDKDKE VISTWGVQNK IDFLSLSYTR HAEDVRQARE
CLSKLGDLYQ TQIFAKIENV EGLTHFDEIL QEADGIILSR GNLGIDLPPE KVFLFQKAAL
YKCNMAGKPA VVTRVVDSMT GNLRPTRAEA TDVANAVLDG SDAILLGAET LRGLYPVETI
STVGKICAEV RAAIKVKASV IICFTSSGRA ARLIAKYRPT MPVLSVVIPR LKTNQLRWSF
SGAFEARQSL IVRGLFPMLA DPRHPAESTS ATNESVLKVA LDHGKASGVI KSHDRVVVCQ
KVGDASVVKI IELED
//
