PPCK2_ARATH
ID PPCK2_ARATH Reviewed; 278 AA.
AC Q93VK0; Q9M834;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphoenolpyruvate carboxylase kinase 2;
DE Short=AtPPCK2;
DE EC=2.7.11.1;
GN Name=PPCK2; OrderedLocusNames=At3g04530; ORFNames=T27C4.19;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT AND CYCLOHEXIMIDE.
RC STRAIN=cv. Landsberg erecta;
RX DOI=10.1046/j.0016-8025.2001.00805.x;
RA Fontaine V., Hartwell J., Jenkins G.I., Nimmo H.G.;
RT "Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase
RT genes with different expression patterns.";
RL Plant Cell Environ. 25:115-122(2002).
RN [2]
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 [3]
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 [4]
RP INDUCTION BY CARBON; NITROGEN AND PHOSPHITE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18771573; DOI=10.1111/j.1365-3040.2008.01885.x;
RA Chen Z.H., Jenkins G.I., Nimmo H.G.;
RT "pH and carbon supply control the expression of phosphoenolpyruvate
RT carboxylase kinase genes in Arabidopsis thaliana.";
RL Plant Cell Environ. 31:1844-1850(2008).
RN [5]
RP INDUCTION BY PHOSPHATE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19228119; DOI=10.1042/bj20082397;
RA Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M.,
RA Knowles V.L., Plaxton W.C.;
RT "In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase
RT AtPPC1 in phosphate-starved Arabidopsis thaliana.";
RL Biochem. J. 420:57-65(2009).
CC -!- FUNCTION: Calcium-independent kinase involved in light-dependent
CC phosphoenolpyruvate carboxylase phosphorylation. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|Ref.1};
CC -!- TISSUE SPECIFICITY: Expressed in flowers and roots, and at lower levels
CC in cauline leaves. Barely detectable in rosette leaves and stems.
CC {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Up-regulated by light, cycloheximide, phosphate starvation,
CC carbon availability and high pH. Down-regulated by phosphate and
CC phosphite. Very high sensitivity to phosphate at low pH. Not under
CC circadian control and not affected by nitrogen supply.
CC {ECO:0000269|PubMed:18771573, ECO:0000269|PubMed:19228119,
CC ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: Lacks the autoinhibitory region and EF hands found in
CC calcium-dependent protein kinases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63784.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF358915; AAK43710.1; -; mRNA.
DR EMBL; AY040830; AAK84668.1; -; Genomic_DNA.
DR EMBL; AC022287; AAF63784.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74093.1; -; Genomic_DNA.
DR RefSeq; NP_566229.1; NM_111324.4.
DR AlphaFoldDB; Q93VK0; -.
DR SMR; Q93VK0; -.
DR BioGRID; 4944; 1.
DR IntAct; Q93VK0; 1.
DR STRING; 3702.AT3G04530.1; -.
DR PaxDb; Q93VK0; -.
DR PRIDE; Q93VK0; -.
DR EnsemblPlants; AT3G04530.1; AT3G04530.1; AT3G04530.
DR GeneID; 819609; -.
DR Gramene; AT3G04530.1; AT3G04530.1; AT3G04530.
DR KEGG; ath:AT3G04530; -.
DR Araport; AT3G04530; -.
DR TAIR; locus:2100875; AT3G04530.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q93VK0; -.
DR OMA; ECIETEP; -.
DR OrthoDB; 330091at2759; -.
DR BioCyc; ARA:AT3G04530-MON; -.
DR BRENDA; 4.1.1.49; 399.
DR PRO; PR:Q93VK0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93VK0; baseline and differential.
DR Genevisible; Q93VK0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0046898; P:response to cycloheximide; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Pyruvate; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..278
FT /note="Phosphoenolpyruvate carboxylase kinase 2"
FT /id="PRO_0000403719"
FT DOMAIN 11..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 48
FT /note="I -> T (in Ref. 1; AAK43710/AAK84668)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="S -> R (in Ref. 1; AAK43710/AAK84668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31199 MW; E6861291838AE6EC CRC64;
MTREFELENN YQLCDEIGRG RFGTITRCFS PATKEFYACK TIDKRVLIDA LDRECIETEP
RIMAMLPPHP NIIRIFDLYE TEDSLAIVME LVDPPMTIYD RLISAGGRLS ESESASYAKQ
ILSALAHCHR CDVVHRDVKP DNVLVDLVSG GVKLCDFGSA VWLGGETAEG VVGTPYYVAP
EVVMGRKYDE KVDIWSAGVV IYTMLAGEPP FNGETAEDIF ESILRGNLRF PPKKFGSVSS
EAKDLLRKMI CRDVSRRFSA EDALRHSWMM NVGNLQSN
