PKP4_ARATH
ID PKP4_ARATH Reviewed; 710 AA.
AC Q9M3B6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Plastidial pyruvate kinase 4, chloroplastic;
DE Short=PKp4;
DE EC=2.7.1.40;
DE Flags: Precursor;
GN Name=PKP4; OrderedLocusNames=At3g49160; ORFNames=F2K15.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=17557808; DOI=10.1105/tpc.106.048629;
RA Andre C., Froehlich J.E., Moll M.R., Benning C.;
RT "A heteromeric plastidic pyruvate kinase complex involved in seed oil
RT biosynthesis in Arabidopsis.";
RL Plant Cell 19:2006-2022(2007).
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q9LIK0};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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; AL132956; CAB66395.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78506.1; -; Genomic_DNA.
DR EMBL; AY072177; AAL59999.1; -; mRNA.
DR EMBL; AY096527; AAM20177.1; -; mRNA.
DR PIR; T45821; T45821.
DR RefSeq; NP_190485.1; NM_114775.3.
DR AlphaFoldDB; Q9M3B6; -.
DR SMR; Q9M3B6; -.
DR BioGRID; 9395; 8.
DR IntAct; Q9M3B6; 7.
DR STRING; 3702.AT3G49160.1; -.
DR PaxDb; Q9M3B6; -.
DR EnsemblPlants; AT3G49160.1; AT3G49160.1; AT3G49160.
DR GeneID; 824077; -.
DR Gramene; AT3G49160.1; AT3G49160.1; AT3G49160.
DR KEGG; ath:AT3G49160; -.
DR Araport; AT3G49160; -.
DR TAIR; locus:2082866; AT3G49160.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_6_0_1; -.
DR InParanoid; Q9M3B6; -.
DR OMA; PVVWATQ; -.
DR OrthoDB; 660707at2759; -.
DR PhylomeDB; Q9M3B6; -.
DR BioCyc; ARA:AT3G49160-MON; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:Q9M3B6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3B6; baseline and differential.
DR Genevisible; Q9M3B6; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR Gene3D; 3.20.20.60; -; 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; PTHR11817; 1.
DR Pfam; PF00224; PK; 2.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plastid; Potassium; Pyruvate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..710
FT /note="Plastidial pyruvate kinase 4, chloroplastic"
FT /id="PRO_0000416990"
FT BINDING 88..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 267
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 299
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 583
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 615
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 647
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 583
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P14618"
SQ SEQUENCE 710 AA; 77827 MW; 515D788AD6609E70 CRC64;
MVGLDSSHLL RDKILCFSSR SHINNQHKKT SYALSLNHMK LPIQRTLAFA LARGKGEAES
FSRLEATFGD NTSTECTWSF DFPDSKDAMS HLKSEADLSG SNGANNVASV IEKLNALRSH
LLAAEKWNAS QLHLCDSKYL ECATNLVHYM ALRSLDIEQL NSHLASLGLS SLDNNNLDVL
AHLNASINLL MNDQNAVTES WTNVYPKGKS TKKNDKGRVL SYKESLLGKL REGRSTHIMV
TIGEEATLSE TFITDILKAG TSVIRINCAH GDPSIWGEII KRVRRTSQML EMPCRVHMDL
AGPKLRTGTL KPGPCVMKIS PKKDAYGNVV SPALVWLCLT GTEPPAHVSP DATISVQGQD
FLAGLQIGDS IRLCDARGRK RRLKISKEFH VFNSTGFVAE CFDTAYIESG TELSVKGKKG
RRLVGRVVDV PPKESFVRLK VGDLLVITRE GSLDEPSVTV PGAHRLTCPS GYLFDSVKPG
ETIGFDDGKI WGVIKGTSPS EVIVSITHAR PKGTKLGSEK SINIPQSDIH FKGLTSKDIK
DLDYVASHAD MVGISFIRDV HDITVLRQEL KKRKLDDLGI VLKIETKSGF KNLSLILLEA
MKCSNPLGIM IARGDLAVEC GWERLANMQE EIIAICKAAR VPVIMATQVL ESLVKSGVPT
RAEITDAANA KRASCVMLNK GKNIVEAVSM LDTILHTKLI YKKSDSENLH
