KAD1_ORYSJ
ID KAD1_ORYSJ Reviewed; 293 AA.
AC Q10S93; A0A0P0VSL2; Q9SNJ4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable adenylate kinase 1, chloroplastic;
DE EC=2.7.4.3;
DE AltName: Full=Adenylate monophosphate kinase 1;
DE Flags: Precursor;
GN OrderedLocusNames=Os03g0130400, LOC_Os03g03820;
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA85412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000615; BAA85412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF93799.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10768.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82125.1; -; Genomic_DNA.
DR EMBL; AK070255; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015627822.1; XM_015772336.1.
DR AlphaFoldDB; Q10S93; -.
DR SMR; Q10S93; -.
DR STRING; 4530.OS03T0130400-01; -.
DR PaxDb; Q10S93; -.
DR PRIDE; Q10S93; -.
DR EnsemblPlants; Os03t0130400-01; Os03t0130400-01; Os03g0130400.
DR GeneID; 4331502; -.
DR Gramene; Os03t0130400-01; Os03t0130400-01; Os03g0130400.
DR KEGG; osa:4331502; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_2_1_1; -.
DR InParanoid; Q10S93; -.
DR OMA; NYKITRR; -.
DR OrthoDB; 1004067at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q10S93; baseline and differential.
DR Genevisible; Q10S93; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants.
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:0008652; P:cellular amino acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048364; P:root development; IEA:EnsemblPlants.
DR GO; GO:0048367; P:shoot system development; IEA:EnsemblPlants.
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; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..293
FT /note="Probable adenylate kinase 1, chloroplastic"
FT /id="PRO_0000430116"
FT REGION 90..119
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 183..231
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 70..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 91
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 96
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 117..119
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147..150
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 154
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 193..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 228
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 239
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT CONFLICT 172
FT /note="L -> S (in Ref. 5; AK070255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31731 MW; 6A7E18E3324B27C5 CRC64;
MAAVQRLLRA SASGGAAAAA AAARRRMSTA VAPEQTPAAA AFPFAAAAGR ARQRVAEERN
VQWVFLGCPG VGKGTYASRL SRLLGVPHIA TGDLVRDELA SSGPLSVQLA EIVNQGKLVS
DEIIINLLSK RLKKGEEQGE SGFILDGFPR TVKQAEILDG VTDIDMVVNL KLREDVLVEK
CLGRRICGQC GKNFNLACID VKGENGLPPI YMAPLLPPNN CMSKLITRAD DTEEVVRNRL
QIYNDMSQPV EGFYRQQGKL LEFDLPGGIP ESWPKLLHVL NLEDQEEMKL ATA
