KAD4_ARATH
ID KAD4_ARATH Reviewed; 246 AA.
AC O82514; Q9FMW2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Adenylate kinase 4;
DE Short=AK 4;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase 4;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase 4;
DE Short=AMK4;
GN Name=ADK1; OrderedLocusNames=At5g63400; ORFNames=MLE2.3;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Weers B., Thornburg R.;
RT "Characterization of the cDNA and gene for the Arabidopsis thaliana
RT adenylate kinase.";
RL (er) Plant Gene Register PGR98-166(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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.
CC {ECO:0000250|UniProtKB:P69441}.
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:0000250|UniProtKB:P69441};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69441}.
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=O82514-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AF082882; AAC78478.1; -; mRNA.
DR EMBL; AB007649; BAB08805.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97743.1; -; Genomic_DNA.
DR EMBL; AY039945; AAK64049.1; -; mRNA.
DR EMBL; AY079340; AAL85071.1; -; mRNA.
DR EMBL; AY085188; AAM61739.1; -; mRNA.
DR RefSeq; NP_201145.1; NM_125735.4. [O82514-1]
DR AlphaFoldDB; O82514; -.
DR SMR; O82514; -.
DR BioGRID; 21702; 2.
DR STRING; 3702.AT5G63400.1; -.
DR iPTMnet; O82514; -.
DR PaxDb; O82514; -.
DR PRIDE; O82514; -.
DR ProteomicsDB; 232240; -. [O82514-1]
DR EnsemblPlants; AT5G63400.1; AT5G63400.1; AT5G63400. [O82514-1]
DR GeneID; 836459; -.
DR Gramene; AT5G63400.1; AT5G63400.1; AT5G63400. [O82514-1]
DR KEGG; ath:AT5G63400; -.
DR Araport; AT5G63400; -.
DR TAIR; locus:2167316; AT5G63400.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_1_0_1; -.
DR OMA; FHNRMRV; -.
DR PhylomeDB; O82514; -.
DR BioCyc; ARA:AT5G63400-MON; -.
DR BRENDA; 2.7.4.3; 399.
DR PRO; PR:O82514; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82514; baseline and differential.
DR Genevisible; O82514; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 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 Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..246
FT /note="Adenylate kinase 4"
FT /id="PRO_0000158940"
FT REGION 63..92
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 159..196
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 43..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 69
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 90..92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 118..121
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 125
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 193
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 144..152
FT /note="LNFAIDDAI -> STLLLMTQS (in Ref. 1; AAC78478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26932 MW; 659903FBD84B39C7 CRC64;
MATGGAAADL EDVQTVDLMS ELLRRLKCSQ KPDKRLIFIG PPGSGKGTQS PVVKDEYCLC
HLSTGDMLRA AVASKTPLGV KAKEAMEKGE LVSDDLVVGI IDEAMNKPKC QKGFILDGFP
RTVTQAEKLD EMLKRRGTEI DKVLNFAIDD AILEERITGR WIHPSSGRSY HTKFAPPKTP
GVDDITGEPL IQRKDDNADV LKSRLAAFHS QTQPVIDYYA KKAVLTNIQA EKAPQEVTSE
VKKALS
