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Database: UniProt
Entry: A0A0D3A9D8_BRAOL
LinkDB: A0A0D3A9D8_BRAOL
Original site: A0A0D3A9D8_BRAOL 
ID   A0A0D3A9D8_BRAOL        Unreviewed;       722 AA.
AC   A0A0D3A9D8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE            EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN   Name=106319996 {ECO:0000313|EnsemblPlants:Bo1g078680.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g078680.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo1g078680.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo1g078680.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663}.
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DR   RefSeq; XP_013613849.1; XM_013758395.1.
DR   RefSeq; XP_013613895.1; XM_013758441.1.
DR   AlphaFoldDB; A0A0D3A9D8; -.
DR   STRING; 109376.A0A0D3A9D8; -.
DR   EnsemblPlants; Bo1g078680.1; Bo1g078680.1; Bo1g078680.
DR   GeneID; 106319996; -.
DR   Gramene; Bo1g078680.1; Bo1g078680.1; Bo1g078680.
DR   KEGG; boe:106319996; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   HOGENOM; CLU_015439_6_0_1; -.
DR   OMA; VWATQVL; -.
DR   OrthoDB; 454163at2759; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000032141; Chromosome C1.
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; 2.
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   PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000032141};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          245..331
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          483..691
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
SQ   SEQUENCE   722 AA;  79495 MW;  B63AA76858BA19A0 CRC64;
     MTSYMSSAPS VTNLWTTPNN VIQLADMVST ESYHLLSGKK TLIFSLRPTK SFPLSLTQMK
     IRVPRTLAFA SAKGKGKAES GVEAIVGDNK SSTERNWSFD FPESKAEFCL VDSEAYQNLS
     SVLEKLNALR SHLLAAKKWN ASRLQSCDSK YLECATNLIH YMALRSLDTE QLNNYLASLG
     LSSLDNDNNL SVLSNLDATI NLLMKSPMES WKQQKGNKII EKNDKGRVLS SYKESLLLGK
     LREGKKTHIM VTVGKEATES ETFITDILKA GASVIRINCA HGDPTLWGEI IKRVRRTSQM
     LEMPCRILMD LAGPKLRTGT LKPGPCVMKV SPKKDAYGNV ASPAIVWLSV TETEPPAHLS
     PDATIFVQDQ EFLAGLQIGD SVRLYDARGK KKKLRISKEF DVFSSTGFVA ECFDTAYVEP
     GTELCVKGNK GRRLFGEVVD VPPKESFVRL RVGDLLVITR EGSFDEPSVT VPGAHRLTCP
     SGYLFDSVKP GETIGFDDGK IWGTIKGASP AEVIVSITHA GPKGTKLGSE KSINIPQSDI
     RFKGLTSKDI KDLEYVASHA DMVGISFIRD VQDITVLRQE LKKRKLNDQL GVVLKIETES
     GFENLPLILL EAMKCLNPLG VMIARGDLAV ECGWERLANL QEEIMAICKV ARMPVILATQ
     VLESLVKSGV PTRAEITDAA NGRRASCVML NKGKHIVEAV SMLDTILHTK LIYKKQESEN
     LH
//
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