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KAD7_ORYSJ
ID   KAD7_ORYSJ              Reviewed;         299 AA.
AC   Q6ZJ48; A0A0P0XBX1;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable adenylate kinase 7, mitochondrial;
DE            EC=2.7.4.3 {ECO:0000250|UniProtKB:P69441};
DE   AltName: Full=Adenylate monophosphate kinase 7;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os08g0118900, LOC_Os08g02540;
GN   ORFNames=OJ1005_B05.19, OsJ_25843;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR   EMBL; AP003925; BAD09046.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF22783.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT03575.1; -; Genomic_DNA.
DR   EMBL; CM000145; EEE67947.1; -; Genomic_DNA.
DR   EMBL; AK109749; BAG98885.1; -; mRNA.
DR   RefSeq; XP_015648647.1; XM_015793161.1.
DR   AlphaFoldDB; Q6ZJ48; -.
DR   SMR; Q6ZJ48; -.
DR   STRING; 4530.OS08T0118900-01; -.
DR   PaxDb; Q6ZJ48; -.
DR   PRIDE; Q6ZJ48; -.
DR   EnsemblPlants; Os08t0118900-01; Os08t0118900-01; Os08g0118900.
DR   GeneID; 4344534; -.
DR   Gramene; Os08t0118900-01; Os08t0118900-01; Os08g0118900.
DR   KEGG; osa:4344534; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   HOGENOM; CLU_032354_2_0_1; -.
DR   InParanoid; Q6ZJ48; -.
DR   OMA; DRGAKKH; -.
DR   OrthoDB; 1004067at2759; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000007752; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; Q6ZJ48; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..299
FT                   /note="Probable adenylate kinase 7, mitochondrial"
FT                   /id="PRO_0000430119"
FT   REGION          100..129
FT                   /note="NMP"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   REGION          193..237
FT                   /note="LID"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         80..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         106
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         127..129
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         157..160
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         164
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         203..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
SQ   SEQUENCE   299 AA;  32821 MW;  4CDC310B4FFA9B09 CRC64;
     MAGVLRLAGA ARSPLARALA PAARRMGASA AAAMEDEAYW TEWEEEEEKA RARESAPVAE
     MCPTGGGGGG PQWVVMGRPG PQKHAHAARL AEVLAVPYIS MGTLVRQELS PASSLYKKIA
     NSVNEGKLVP EDIIFGLLTK RLEEGYNKGE TGFILDGIPR THMQAEILDE IVDIDLVLNF
     KCADNCFMKR RFGGDICPHC GQLFDFSKTA SSDRNPSLGS CTWPSQVQHA AVLGLEDSRM
     EKMRAYAEQT KLLEDYYRKQ RKLMELKTSA RPGETWQGLV AALHLQHLDA SPTPHKLTM
 
 
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