KAD5_ARATH
ID KAD5_ARATH Reviewed; 588 AA.
AC Q8VYL1; Q9FYQ6; Q9FYQ7;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Adenylate kinase 5, chloroplastic;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase 5;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase 5;
DE Short=AMK5;
DE Flags: Precursor;
GN OrderedLocusNames=At5g35170; ORFNames=T25C13.50;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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. {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
CC {ECO:0000269|PubMed:18162585}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8VYL1-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18162585}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AP000421; BAB10023.1; -; Genomic_DNA.
DR EMBL; AP002031; BAB11193.1; -; Genomic_DNA.
DR EMBL; AP000421; BAB11193.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED93936.1; -; Genomic_DNA.
DR EMBL; AY070456; AAL49859.1; -; mRNA.
DR EMBL; AY133763; AAM91697.1; -; mRNA.
DR EMBL; AK226238; BAE98401.1; -; mRNA.
DR RefSeq; NP_198367.2; NM_122908.4. [Q8VYL1-1]
DR AlphaFoldDB; Q8VYL1; -.
DR SMR; Q8VYL1; -.
DR BioGRID; 18726; 1.
DR STRING; 3702.AT5G35170.1; -.
DR iPTMnet; Q8VYL1; -.
DR PaxDb; Q8VYL1; -.
DR PRIDE; Q8VYL1; -.
DR ProteomicsDB; 250628; -. [Q8VYL1-1]
DR EnsemblPlants; AT5G35170.1; AT5G35170.1; AT5G35170. [Q8VYL1-1]
DR GeneID; 833471; -.
DR Gramene; AT5G35170.1; AT5G35170.1; AT5G35170. [Q8VYL1-1]
DR KEGG; ath:AT5G35170; -.
DR Araport; AT5G35170; -.
DR TAIR; locus:2182407; AT5G35170.
DR eggNOG; KOG3078; Eukaryota.
DR InParanoid; Q8VYL1; -.
DR OMA; DMRLKYA; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; Q8VYL1; -.
DR BioCyc; ARA:AT5G35170-MON; -.
DR BRENDA; 2.7.4.3; 399.
DR PRO; PR:Q8VYL1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYL1; baseline and differential.
DR Genevisible; Q8VYL1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; 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: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; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR018962; DUF1995.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF09353; DUF1995; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Kinase; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..73
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 74..588
FT /note="Adenylate kinase 5, chloroplastic"
FT /id="PRO_0000430114"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..138
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 202..235
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 89..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 115
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 136..138
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 165..168
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 232
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 243
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 588 AA; 65738 MW; 3AA0B81ABFC4B62B CRC64;
MASLSLSSAH FSSTSSSSRS SISTSSLSPS STSLPLLQSP IRRRYRSLRR RLSFSVIPRR
TSRSFSTSNS QIRCSINEPL KVMISGAPAS GKGTQCELIV HKFGLVHIST GDLLRAEVSS
GTDIGKRAKE FMNSGSLVPD EIVIAMVAGR LSREDAKEHG WLLDGFPRSF AQAQSLDKLN
VKPDIFILLD VPDEILIDRC VGRRLDPVTG KIYHIKNYPP ESDEIKARLV TRPDDTEEKV
KARLQIYKQN SEAIISAYSD VMVKIDANRP KEVVFEETQT LLSQIQLKRM IKTDKASPVQ
DKWRGIPTRL NNIPHSRDIR AYFYEDVLQA TIRSIKDGNT RLRVDINIPE LNPEMDVYRI
GTLMELVQAL ALSFADDGKR VKVCVQGSMG EGALAGMPLQ LAGTRKILEY MDWGDDETLG
TFVKLGAIGG KEVDEEDDMF ILVAPQNAVG NCIIDDLQAM TTAAGKRPVV LINPRLKDLP
ASSGIMQTMG REQRLEYALT FDNCYVFRLL YYLGTQYPIM GALRMSYPYR YELYKRVNEE
NGKEKYVLLA TYAERPTPEQ IDDAFSGKSR DQSKKASGIW GFLSSVFS
