KAD2_ARATH
ID KAD2_ARATH Reviewed; 283 AA.
AC Q9FIJ7;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Adenylate kinase 2, chloroplastic;
DE Short=AK 2;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase 2;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase 2;
DE Short=AMK2;
DE Flags: Precursor;
GN OrderedLocusNames=At5g47840; ORFNames=MCA23.18;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18162585; DOI=10.1104/pp.107.114702;
RA Lange P.R., Geserick C., Tischendorf G., Zrenner R.;
RT "Functions of chloroplastic adenylate kinases in Arabidopsis.";
RL Plant Physiol. 146:492-504(2008).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. Plays a major role in
CC the equilibration of adenylates and de novo synthesis of ADP in the
CC plastid stroma. {ECO:0000269|PubMed:18162585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000269|PubMed:18162585};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18162585}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality when homozygous, due to loss
CC of chloroplast integrity, causing a bleached phenotype from early
CC embryo to seedling development. {ECO:0000269|PubMed:18162585}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AB016886; BAB11331.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95579.1; -; Genomic_DNA.
DR EMBL; AY049305; AAK83647.1; -; mRNA.
DR EMBL; BT001036; AAN46790.1; -; mRNA.
DR RefSeq; NP_199595.1; NM_124158.4.
DR AlphaFoldDB; Q9FIJ7; -.
DR SMR; Q9FIJ7; -.
DR STRING; 3702.AT5G47840.1; -.
DR MetOSite; Q9FIJ7; -.
DR PaxDb; Q9FIJ7; -.
DR PRIDE; Q9FIJ7; -.
DR ProteomicsDB; 250627; -.
DR EnsemblPlants; AT5G47840.1; AT5G47840.1; AT5G47840.
DR GeneID; 834835; -.
DR Gramene; AT5G47840.1; AT5G47840.1; AT5G47840.
DR KEGG; ath:AT5G47840; -.
DR Araport; AT5G47840; -.
DR TAIR; locus:2160942; AT5G47840.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_6_0_1; -.
DR InParanoid; Q9FIJ7; -.
DR OMA; EVVVEMV; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; Q9FIJ7; -.
DR BioCyc; ARA:AT5G47840-MON; -.
DR BRENDA; 2.7.4.3; 399.
DR PRO; PR:Q9FIJ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIJ7; baseline and differential.
DR Genevisible; Q9FIJ7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IBA:GO_Central.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..283
FT /note="Adenylate kinase 2, chloroplastic"
FT /id="PRO_0000016555"
FT REGION 94..123
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 187..220
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 74..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 100
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 121..123
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 150..153
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 157
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 217
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 228
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 283 AA; 31452 MW; 1461D1A36F2DF4E9 CRC64;
MTGCVNSISP PPVTLYRHRA SPSRSSFSLS GDALHSLYRH RRVSRSPSII APKFQIVAAE
KSEPLKIMIS GAPASGKGTQ CELITHKYGL VHISAGDLLR AEIASGSENG RRAKEHMEKG
QLVPDEIVVM MVKDRLSQTD SEQKGWLLDG YPRSASQATA LKGFGFQPDL FIVLEVPEEI
LIERVVGRRL DPVTGKIYHL KYSPPETEEI AVRLTQRFDD TEEKAKLRLK THNQNVSDVL
SMYDDITIKI EGNRSKEEVF AQIDSSLSEL LQERNTAPSS LLS
