GenomeNet

Database: UniProt
Entry: A0A0D2W3G7_GOSRA
LinkDB: A0A0D2W3G7_GOSRA
Original site: A0A0D2W3G7_GOSRA 
ID   A0A0D2W3G7_GOSRA        Unreviewed;       340 AA.
AC   A0A0D2W3G7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=B456_013G066700 {ECO:0000313|EMBL:KJB79785.1}, Gorai_002458
GN   {ECO:0000313|EMBL:MBA0602272.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB79785.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB79785.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
RN   [2] {ECO:0000313|EMBL:MBA0602272.1, ECO:0000313|Proteomes:UP000593578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:MBA0602272.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:MBA0602272.1};
RX   PubMed=30476109;
RA   Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA   Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA   Wendel J.F.;
RT   "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT   Subgenus Houzingenia) Based on Genome Sequencing.";
RL   Genome Biol. Evol. 11:53-71(2019).
RN   [3] {ECO:0000313|EMBL:MBA0602272.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=8 {ECO:0000313|EMBL:MBA0602272.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:MBA0602272.1};
RA   Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA   Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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; CM001752; KJB79783.1; -; Genomic_DNA.
DR   EMBL; CM001752; KJB79784.1; -; Genomic_DNA.
DR   EMBL; CM001752; KJB79785.1; -; Genomic_DNA.
DR   EMBL; CM001752; KJB79786.1; -; Genomic_DNA.
DR   EMBL; JABEZZ010000013; MBA0602272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2W3G7; -.
DR   EnsemblPlants; KJB79783; KJB79783; B456_013G066700.
DR   EnsemblPlants; KJB79784; KJB79784; B456_013G066700.
DR   EnsemblPlants; KJB79785; KJB79785; B456_013G066700.
DR   EnsemblPlants; KJB79786; KJB79786; B456_013G066700.
DR   Gramene; KJB79783; KJB79783; B456_013G066700.
DR   Gramene; KJB79784; KJB79784; B456_013G066700.
DR   Gramene; KJB79785; KJB79785; B456_013G066700.
DR   Gramene; KJB79786; KJB79786; B456_013G066700.
DR   OMA; THEYHAS; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000032304; Chromosome 13.
DR   Proteomes; UP000593578; 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; 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:SF3; AT14039P-RELATED; 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; 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:UP000032304};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          2..175
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          210..328
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   340 AA;  36789 MW;  3A5D35999667E0F6 CRC64;
     MIGERKNVNL PDVVVDLPML TEKDKEDILG WGVPNNIDMI AFSFVRKGSD LVNVNKVFGP
     NAKQIQLMSK VENQEGVINF DEILCETDAF MVTRGDLGME ILIEKIFLAQ KMMIYKCNLA
     DKPVVTATQM LESIIKSPRP THAEATDVAN AVLDGTDCIM LSGESAAGAY PELAVKIISQ
     ICIEAESSLD YGGIFKEMIR STLLPKSPLE SLASSAVRTA NKAKATLIVV LTRGGTIAKL
     VAKYRPAVPI LSVVVPVLTT DSFNWSCSDE WLARHSLIYR GLIPVLAEGS AKATDAESTE
     VILEAAMKSA TKKRLCKPGD AILALHRIGA ASVIKICVVK
//
DBGET integrated database retrieval system