ID A0A398AVW3_BRACM Unreviewed; 722 AA.
AC A0A398AVW3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=BRARA_A02192 {ECO:0000313|EMBL:RID79456.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID79456.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID79456.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM010628; RID79456.1; -; Genomic_DNA.
DR RefSeq; XP_009151832.1; XM_009153584.2.
DR RefSeq; XP_009151838.1; XM_009153590.2.
DR RefSeq; XP_009151847.1; XM_009153599.2.
DR RefSeq; XP_018512308.1; XM_018656792.1.
DR AlphaFoldDB; A0A398AVW3; -.
DR GeneID; 103875118; -.
DR KEGG; brp:103875118; -.
DR OrthoDB; 454163at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000264353; Chromosome a1.
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 Gene3D; 2.40.33.10; PK beta-barrel domain-like; 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 InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 245..330
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; 79212 MW; F74DB72A5C55C4C3 CRC64;
MTSYMSSAPS VTNFWTTPNN VIQLAGMVST ESYHLLSGKK TLIFSLRPTK SFPLSLTQMK
IRVPRTLAFA SAKGKGKAES GVEAAIVGDN NTSTERNWSF DFPESKAEFC LVDSEACQNL
SSVLEKLNAL RSHLLAAEKW NASRLQSCDS KYLECATNLI HYMALRSLDT EQLNSYLASL
SLSSLDNNNK LSVLSNLDAT INLLMKSPME SWKQQKGNKI IQKNDKGRVL SSYKESLLGK
LREGKRTHIM VTVGKEATES ETFITDILKA GASVIRINCA HGDPTIWGEI IKRVRRASQM
LEMPCRVLMD LAGPKLRTGT LKPGPCVMKV SPKKDAYGNV ASPAIVWLSV TGTEPPPHLS
PDATMFVQDH EFLAGLQIGD SVRLYDARGK KKKLRISKEF DVFSSTGFVA ECFDTAYVES
GTELCVKGNR GRRLFGEVVD VPPKESFVRL RVGDLLVITR EGSFDEPSVT VPGAHRLTCP
SGYLFDSVKP GETIGFDDGK IWGTIKGASP AEVIVSITHA GPKGTKLGSE KSINIPQSDI
RFKGLTSKDI KDLEYVASHA DMVGISFIRD VQDITVLRQE LKKRKLNDQL GVVLKIETES
GFENLPLILL EAMKCLNPLG VMIARGDLAV ECGWERLANI QEEIMAICKI ARVPVILATQ
VLESLVKSGV PTRAEITDAA SGRRASCVML NKGKHITEAV SMLDTILHTK LTYKKLDSGN
LH
//
