ID A0A4U5NRV1_POPAL Unreviewed; 568 AA.
AC A0A4U5NRV1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=D5086_0000246530 {ECO:0000313|EMBL:TKR85511.1};
OS Populus alba (White poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335 {ECO:0000313|EMBL:TKR85511.1, ECO:0000313|Proteomes:UP000309997};
RN [1] {ECO:0000313|Proteomes:UP000309997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PAL-ZL1 {ECO:0000313|Proteomes:UP000309997};
RX PubMed=30661181; DOI=10.1007/s11427-018-9455-2;
RA Liu Y.-J., Wang X.-R., Zeng Q.-Y.;
RT "De novo assembly of white poplar genome and genetic diversity of white
RT poplar population in Irtysh River basin in China.";
RL Sci. China Life Sci. 62:609-618(2019).
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:TKR85511.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCHU01000939; TKR85511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5NRV1; -.
DR STRING; 43335.A0A4U5NRV1; -.
DR OrthoDB; 601at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000309997; Unassembled WGS sequence.
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; 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 NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF63; PLASTIDIAL PYRUVATE KINASE 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; 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.
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, ECO:0000313|EMBL:TKR85511.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000309997};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 98..418
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 456..546
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 568 AA; 63051 MW; 08C7816E3DC246E9 CRC64;
MATINNMSTI MCRDHRSLSS SSKLSDVFML ESRLRKRCFF QNPNFTVRSM KVREQNQTAN
LVSSNGSLTA SDKVNPPLEL LTNSQTLVKE KTNPISRRKT KIVCTIGPST SSREMIWKLA
EAGMNVARLN MSHGDHASHK ITIDLVKEYN AQSDDNVIAI MLDTKGPEVR SGDVPQPIIL
EEGKEFNFTI KRGVSSEDTV SVNYDDFIND VEVGDMILVD GGMMSLAVKS KTNDLVKCVV
VDGGELKSRR HLNVRGKSAT LPSITDKDWE DIKFGVDNQV DFYAVSFVKD AEVVHELKDY
LKSCNADIHV IVKIESADSI PNLHSIISAS DGAMVARGDL GAELPIEEVP LLQEDIIRRC
HSMQKPVIVA TNMLESMIDH PTPTRAEVSD IAIAVREGAD AVMLSGETAH GKYPLKAVKV
MHTVALRTES SLPVNTTAPT HTVYQSHMGE MFAFHATIMA NTLNTPIIVF TRTGSMAIHL
SHFRPSSTIF AFTNEERIKQ RLALYQGVMP IYMQFSDNAE ETFSRALKLL LNKDQLMEGQ
HVTLVQSGAQ PIWRLKSTHH IQVCKVQS
//
