KAD6_ARATH
ID KAD6_ARATH Reviewed; 178 AA.
AC Q9FJI1; C0Z207;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
GN Name=AAK6; OrderedLocusNames=At5g60340; ORFNames=K9B18.5;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(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] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH RPS14A.
RX PubMed=23121860; DOI=10.1016/j.plaphy.2012.10.002;
RA Feng X., Yang R., Zheng X., Zhang F.;
RT "Identification of a novel nuclear-localized adenylate kinase 6 from
RT Arabidopsis thaliana as an essential stem growth factor.";
RL Plant Physiol. Biochem. 61:180-186(2012).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates. Preferred
CC phosphate donor and acceptor are ATP and AMP, respectively. Has also
CC ATPase activity (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:23121860}.
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:0000255|HAMAP-Rule:MF_03173,
CC ECO:0000269|PubMed:23121860};
CC -!- SUBUNIT: Interacts with RPS14A. {ECO:0000269|PubMed:23121860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03173,
CC ECO:0000269|PubMed:23121860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FJI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FJI1-2; Sequence=VSP_045290, VSP_045291;
CC -!- DISRUPTION PHENOTYPE: Decreased stem growth.
CC {ECO:0000269|PubMed:23121860}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
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DR EMBL; AB015471; BAB10972.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97311.1; -; Genomic_DNA.
DR EMBL; AY079019; AAL84974.1; -; mRNA.
DR EMBL; AY093748; AAM10372.1; -; mRNA.
DR EMBL; AK117598; BAC42255.1; -; mRNA.
DR EMBL; AK318621; BAH56736.1; -; mRNA.
DR RefSeq; NP_200842.2; NM_125427.3. [Q9FJI1-1]
DR AlphaFoldDB; Q9FJI1; -.
DR SMR; Q9FJI1; -.
DR BioGRID; 21400; 8.
DR IntAct; Q9FJI1; 11.
DR STRING; 3702.AT5G60340.1; -.
DR PaxDb; Q9FJI1; -.
DR PRIDE; Q9FJI1; -.
DR ProteomicsDB; 232297; -. [Q9FJI1-1]
DR EnsemblPlants; AT5G60340.1; AT5G60340.1; AT5G60340. [Q9FJI1-1]
DR GeneID; 836156; -.
DR Gramene; AT5G60340.1; AT5G60340.1; AT5G60340. [Q9FJI1-1]
DR KEGG; ath:AT5G60340; -.
DR Araport; AT5G60340; -.
DR TAIR; locus:2158299; AT5G60340.
DR eggNOG; KOG3347; Eukaryota.
DR HOGENOM; CLU_079096_3_1_1; -.
DR InParanoid; Q9FJI1; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 1488235at2759; -.
DR BioCyc; ARA:AT5G60340-MON; -.
DR PRO; PR:Q9FJI1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJI1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0080186; P:developmental vegetative growth; IMP:UniProtKB.
DR GO; GO:0046939; P:nucleotide phosphorylation; IDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein;
KW Growth regulation; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..178
FT /note="Adenylate kinase isoenzyme 6 homolog"
FT /id="PRO_0000421171"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..66
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 118..128
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 23..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 49
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT VAR_SEQ 120..127
FT /note="GYSGTKLS -> SDFQIHQM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_045290"
FT VAR_SEQ 128..178
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_045291"
SQ SEQUENCE 178 AA; 20444 MW; E0A3446FB10C0F4B CRC64;
MARRNRGVTR RERPNLLITG TPGTGKSTTA SALAEATNLR YICIGDLVKE KEFYHGWDNE
LECHFINEDS VIDELDDAMI EGGNIVDYHG CDFFPQRWFD RVVVLRTENS VLYDRLTNRG
YSGTKLSNNL QCEMYQVLLE EAHDSYDEEI VTELQSNTIE DISNNVSTLT DWINAWQP
