KAD1_ARATH
ID KAD1_ARATH Reviewed; 284 AA.
AC Q9ZUU1;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Adenylate kinase 1, chloroplastic;
DE Short=AK 1;
DE Short=AtPADK1;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase 1;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase 1;
DE Short=AMK1;
DE Flags: Precursor;
GN Name=ADK; OrderedLocusNames=At2g37250; ORFNames=F3G5.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15618410; DOI=10.1104/pp.104.056143;
RA Carrari F., Coll-Garcia D., Schauer N., Lytovchenko A., Palacios-Rojas N.,
RA Balbo I., Rosso M., Fernie A.R.;
RT "Deficiency of a plastidial adenylate kinase in Arabidopsis results in
RT elevated photosynthetic amino acid biosynthesis and enhanced growth.";
RL Plant Physiol. 137:70-82(2005).
RN [6]
RP SUBCELLULAR LOCATION.
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, adenine nucleotide metabolism and plant growth.
CC {ECO:0000269|PubMed:15618410}.
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:15618410};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18162585}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and at lower levels in
CC roots, leaves and stems. {ECO:0000269|PubMed:15618410}.
CC -!- DISRUPTION PHENOTYPE: Enhanced root growth and increased amino acid
CC biosynthetis in the light period. {ECO:0000269|PubMed:15618410}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AC005896; AAC98046.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09372.1; -; Genomic_DNA.
DR EMBL; AY056092; AAL06980.1; -; mRNA.
DR EMBL; AY045694; AAK74052.1; -; mRNA.
DR EMBL; AY052310; AAK96503.1; -; mRNA.
DR EMBL; AY085585; AAM62806.1; -; mRNA.
DR PIR; D84790; D84790.
DR RefSeq; NP_181262.1; NM_129281.5.
DR AlphaFoldDB; Q9ZUU1; -.
DR SMR; Q9ZUU1; -.
DR BioGRID; 3646; 1.
DR STRING; 3702.AT2G37250.1; -.
DR PaxDb; Q9ZUU1; -.
DR PRIDE; Q9ZUU1; -.
DR ProteomicsDB; 232237; -.
DR EnsemblPlants; AT2G37250.1; AT2G37250.1; AT2G37250.
DR GeneID; 818302; -.
DR Gramene; AT2G37250.1; AT2G37250.1; AT2G37250.
DR KEGG; ath:AT2G37250; -.
DR Araport; AT2G37250; -.
DR TAIR; locus:2049842; AT2G37250.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_2_1_1; -.
DR InParanoid; Q9ZUU1; -.
DR OMA; NYKITRR; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; Q9ZUU1; -.
DR BioCyc; ARA:AT2G37250-MON; -.
DR PRO; PR:Q9ZUU1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUU1; baseline and differential.
DR Genevisible; Q9ZUU1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..284
FT /note="Adenylate kinase 1, chloroplastic"
FT /id="PRO_0000016554"
FT REGION 81..110
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 174..222
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 61..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 82
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 108..110
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 138..141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 145
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 219
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 230
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 284 AA; 31038 MW; B7E939E89E080898 CRC64;
MARLVRVARS SSLFGFGNRF YSTSAEASHA SSPSPFLHGG GASRVAPKDR NVQWVFLGCP
GVGKGTYASR LSTLLGVPHI ATGDLVREEL ASSGPLSQKL SEIVNQGKLV SDEIIVDLLS
KRLEAGEARG ESGFILDGFP RTMRQAEILG DVTDIDLVVN LKLPEEVLVD KCLGRRTCSQ
CGKGFNVAHI NLKGENGRPG ISMDPLLPPH QCMSKLVTRA DDTEEVVKAR LRIYNETSQP
LEEYYRTKGK LMEFDLPGGI PESWPRLLEA LRLDDYEEKQ SVAA
