PCKA2_ARATH
ID PCKA2_ARATH Reviewed; 670 AA.
AC B5X574; O49547; Q56X60;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) 2 {ECO:0000303|PubMed:14671017, ECO:0000303|PubMed:17283014};
DE Short=PEP carboxykinase 2 {ECO:0000303|PubMed:14671017, ECO:0000303|PubMed:17283014};
DE Short=PEPCK 2 {ECO:0000303|PubMed:14671017, ECO:0000303|PubMed:17283014};
DE EC=4.1.1.49 {ECO:0000250|UniProtKB:Q9T074};
GN Name=PCK2 {ECO:0000303|PubMed:14671017, ECO:0000303|PubMed:17283014};
GN OrderedLocusNames=At5g65690 {ECO:0000312|Araport:AT5G65690};
GN ORFNames=F6H11.190 {ECO:0000312|EMBL:CAA16690.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-670.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=14671017; DOI=10.1104/pp.103.032938;
RA Moire L., Rezzonico E., Goepfert S., Poirier Y.;
RT "Impact of unusual fatty acid synthesis on futile cycling through beta-
RT oxidation and on gene expression in transgenic plants.";
RL Plant Physiol. 134:432-442(2004).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17283014; DOI=10.1093/pcp/pcm014;
RA Malone S., Chen Z.-H., Bahrami A.R., Walker R.P., Gray J.E., Leegood R.C.;
RT "Phosphoenolpyruvate carboxykinase in Arabidopsis: changes in gene
RT expression, protein and activity during vegetative and reproductive
RT development.";
RL Plant Cell Physiol. 48:441-450(2007).
CC -!- FUNCTION: Involved in the gluconeogenesis (By similarity). Catalyzes
CC the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP)
CC through direct phosphoryl transfer between the nucleoside triphosphate
CC and OAA (By similarity). {ECO:0000250|UniProtKB:Q9T074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000250|UniProtKB:Q9T074};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P22259};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P22259};
CC -!- ACTIVITY REGULATION: Allosterically activated by calcium. It may
CC represent the only case of a monomeric, allosteric enzyme.
CC {ECO:0000250|UniProtKB:P22259}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000250|UniProtKB:P22259}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22259}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9T074}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, seeds, stems and
CC roots. {ECO:0000269|PubMed:17283014}.
CC -!- DEVELOPMENTAL STAGE: Accumulates transiently in germinating seeds (at
CC protein level) with a constant transcript level (PubMed:14671017,
CC PubMed:17283014). Abundant in cotyledons during post-germinative growth
CC and in sink tissues, such as young leaves, developing flowers, siliques
CC and seeds (at protein level) (PubMed:17283014). In flowers, present in
CC the nectaries, stigma, endocarp of the fruit wall and in tissues
CC involved in the transfer of assimilates to the developing ovules and
CC seeds, such as the vasculature and seed coat (at protein level)
CC (PubMed:17283014). {ECO:0000269|PubMed:14671017,
CC ECO:0000269|PubMed:17283014}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10675.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16690.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010075; BAB10675.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021684; CAA16690.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98087.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69779.1; -; Genomic_DNA.
DR EMBL; BT046193; ACI49792.1; -; mRNA.
DR EMBL; AK221817; BAD94014.1; -; mRNA.
DR PIR; T05900; T05900.
DR RefSeq; NP_001331433.1; NM_001345716.1.
DR RefSeq; NP_680468.1; NM_148163.3.
DR AlphaFoldDB; B5X574; -.
DR SMR; B5X574; -.
DR STRING; 3702.AT5G65690.1; -.
DR PaxDb; B5X574; -.
DR PRIDE; B5X574; -.
DR ProteomicsDB; 181666; -.
DR EnsemblPlants; AT5G65690.1; AT5G65690.1; AT5G65690.
DR EnsemblPlants; AT5G65690.4; AT5G65690.4; AT5G65690.
DR GeneID; 836696; -.
DR Gramene; AT5G65690.1; AT5G65690.1; AT5G65690.
DR Gramene; AT5G65690.4; AT5G65690.4; AT5G65690.
DR KEGG; ath:AT5G65690; -.
DR Araport; AT5G65690; -.
DR TAIR; locus:504954890; AT5G65690.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR HOGENOM; CLU_018247_0_1_1; -.
DR InParanoid; B5X574; -.
DR OMA; EHAIKYE; -.
DR PhylomeDB; B5X574; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B5X574; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR PANTHER; PTHR30031; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cytoplasm; Kinase; Lyase; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..670
FT /note="Phosphoenolpyruvate carboxykinase (ATP) 2"
FT /id="PRO_0000450744"
FT REGION 24..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 368..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259,
FT ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 389
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 573..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9T074"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9T074"
FT CONFLICT 600
FT /note="D -> H (in Ref. 5; BAD94014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 72892 MW; D321BB9F8AF5CD10 CRC64;
MAGNGNESTG GDFSFSAAAA RDALPRITTE KGGKSPGPAD VCQDDIAPRV NFQTIDELHS
LQKKRSAPTT PLRDGSASGV SGTSGPTTPV SSETMLQSVS ASLASLTRET GPKLIRGDPT
SAAKVAHVPV TPTSLPAADV SDSGLKFTHI LHNLSPAELY EQAIKFEKGS FVTSTGALAT
LSGAKTGRSP KDKRVVKDDT TEAELWWGKG SPNIEMDEKT FLVNRERAVD YLNSLDKVFV
NDQYLNWDPE NKIKVRIVSA RAYHSLFMHN MCIRPTPEEL ENFGTPDFTI YNAGKFPCNR
FTHYMTSSTS VDINLGRREM VILGTQYAGE MKKGLFGVMH YLMPKRKILS LHSGCNMGKD
GDVALFFGLS GTGKTTLSTD HNRYLIGDDE HCWSEAGVSN IEGGCYAKCI DLARDKEPDI
WNAIKFGTVL ENVVFDEHTR EVDYTDKSVT ENTRAAYPIE YIPNSKIPCV GPHPKNVILL
ACDAFGVLPP ISKLNLAQTM YHFISGYTAL VAGTEEGVKE PRATFSACFG AAFIMLHPTK
YAAMLAEKMQ AQGATGWLVN TGWSGGSYGT GSRIKLAYTR KIIDAIHSGS LLNASYRKTD
IFGLEIPNEV EGVPSEILEP INAWPDKMAY EDTLLKLAGL FKSNFETFTS HKIGDDGKLT
EEILAAGPNF
