KAD2_ORYSJ
ID KAD2_ORYSJ Reviewed; 290 AA.
AC Q6ZC69; A0A0P0XAX0;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable adenylate kinase 2, chloroplastic;
DE EC=2.7.4.3;
DE AltName: Full=Adenylate monophosphate kinase 2;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0109300, LOC_Os08g01770; ORFNames=P0007D08.12;
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 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: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AP004584; BAD09526.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22724.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03486.1; -; Genomic_DNA.
DR EMBL; AK061825; BAG88132.1; -; mRNA.
DR EMBL; AK066688; BAG90082.1; -; mRNA.
DR RefSeq; XP_015649892.1; XM_015794406.1.
DR AlphaFoldDB; Q6ZC69; -.
DR SMR; Q6ZC69; -.
DR STRING; 4530.OS08T0109300-01; -.
DR PaxDb; Q6ZC69; -.
DR PRIDE; Q6ZC69; -.
DR EnsemblPlants; Os08t0109300-01; Os08t0109300-01; Os08g0109300.
DR GeneID; 4344470; -.
DR Gramene; Os08t0109300-01; Os08t0109300-01; Os08g0109300.
DR KEGG; osa:4344470; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_6_1_1; -.
DR InParanoid; Q6ZC69; -.
DR OMA; EVVVEMV; -.
DR OrthoDB; 1004067at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6ZC69; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; 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:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IEA:EnsemblPlants.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..290
FT /note="Probable adenylate kinase 2, chloroplastic"
FT /id="PRO_0000430117"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..132
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 196..229
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 83..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 109
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 130..132
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 159..162
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 166
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 206..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 226
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 237
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 290 AA; 31817 MW; 058918D67A71E8D2 CRC64;
MASSMAATAT LSPPVLSAER PTVRGGLFLP PSPATSRSLR LQSARRCGIS PATRKPRSLP
RAAKVVVAVK ADPLKVMIAG APASGKGTQC ELIKSKYGLV HISAGDLLRA EIAAGSENGK
RAKEFMEKGQ LVPDEIVVNM VKERLLQPDA QEKGWLLDGY PRSYSQAMAL ETLNIRPDIF
ILLDVPDELL VERVVGRRLD PVTGKIYHLK YSPPENEEIA SRLTQRFDDT EEKVKLRLQT
HYQNVESLLS IYEDVIVEVK GDALVDDVFA EIDKQLTSSL DKKTEMVASA
