ID KAD5_ORYSJ Reviewed; 608 AA.
AC Q0J6P7; Q6Z5X4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 27-NOV-2024, entry version 93.
DE RecName: Full=Probable adenylate kinase 5, chloroplastic;
DE EC=2.7.4.3;
DE AltName: Full=Adenylate monophosphate kinase 5;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0288200, LOC_Os08g19140; ORFNames=B1114E07.12;
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] OF 116-608.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD01341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF23368.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005097; BAD01341.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF23368.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK070372; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015648092.1; XM_015792606.1.
DR RefSeq; XP_015648094.1; XM_015792608.1.
DR AlphaFoldDB; Q0J6P7; -.
DR SMR; Q0J6P7; -.
DR STRING; 39947.Q0J6P7; -.
DR PaxDb; 39947-Q0J6P7; -.
DR GeneID; 4345177; -.
DR KEGG; osa:4345177; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_3_1_1; -.
DR InParanoid; Q0J6P7; -.
DR OrthoDB; 143569at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004127; F:(d)CMP kinase activity; 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:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR FunFam; 3.40.50.300:FF:001694; Adenylate kinase, chloroplastic; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR053021; Chloroplast_ADK.
DR InterPro; IPR018962; DUF1995.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR35509:SF6; ADENYLATE KINASE; 1.
DR PANTHER; PTHR35509; DOMAIN PROTEIN, PUTATIVE (DUF1995)-RELATED; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF09353; DUF1995; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..608
FT /note="Probable adenylate kinase 5, chloroplastic"
FT /id="PRO_0000430118"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..148
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 212..245
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 99..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 120
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 146..148
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 175..178
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 182
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 222..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 242
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 253
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 608 AA; 66883 MW; 1802F366CA7001EA CRC64;
MAASSSSSSP AAASAPFAAP GPHRRPGLAL RPSPPTPPSS SLSCCRASPA AAAVSSVSAT
AAPNRGPRGM GLRCRASEGA AAAARKEAPL KVMISGAPAS GKGTQCRMIV EKYGLVHIST
GDLLRAEVSS GTEIGKKAKE YMDNGMLVPD QVVTDMVVSR LSQPDVRERG WLLDGYPRSY
AQAQSLESMK IRPDIFIVLE VPDDILIDRC VGRRLDPETG KIYHIKNFPP ENDEVSARLV
TRSDDTFEKV KSRLDTYKQN SEAVIPTYSD LLNQIDGNRQ VEVVFNEIDS LLQKICENAS
FNMLAKTNGK PQDSKDTTAS KNEFRGIPTR LNNIPHSREI RKYFYNDVLV ATRHAVEDKK
TRLQIDINIP ELNPEMDVYR IGTLMELVRE LSLSFADDGK RVKVCVQGSM GQGAFAGIPL
QLAGTRKILE IMDWGEYGAK GTFINFGAVG ASEVDKEDDM FILIAPQNAV GNCIIDDMKA
MTDAAGDRPV ILVNPRLKDM PGSSGVMQTM GRDMRLKYAA SFETCYSFRL LFYAGSFYPI
MGALRMAYPN KYEIYRRVDE PNGQERYVLL EEFVEKPTPD EITNAFRPRK NENEKSASGF
WGFLSGIL
//
