MTK1_ORYSJ
ID MTK1_ORYSJ Reviewed; 430 AA.
AC Q7XR61; A0A0P0WG57; Q6PMT1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Methylthioribose kinase 1 {ECO:0000303|PubMed:15557090};
DE Short=MTR kinase 1 {ECO:0000303|PubMed:15557090};
DE Short=OsMTK1 {ECO:0000303|PubMed:15557090};
DE EC=2.7.1.100 {ECO:0000269|PubMed:15557090};
GN Name=MTK1 {ECO:0000303|PubMed:15557090};
GN OrderedLocusNames=Os04g0669800 {ECO:0000312|EMBL:BAS91547.1},
GN LOC_Os04g57400 {ECO:0000305};
GN ORFNames=OsJ_16565 {ECO:0000312|EMBL:EAZ32355.1},
GN OSJNBa0043A12.24 {ECO:0000312|EMBL:CAE02819.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=15557090; DOI=10.1104/pp.104.053587;
RA Sauter M., Cornell K.A., Beszteri S., Rzewuski G.;
RT "Functional analysis of methylthioribose kinase genes in plants.";
RL Plant Physiol. 136:4061-4071(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000269|PubMed:15557090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:22312,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:78440, ChEBI:CHEBI:456216; EC=2.7.1.100;
CC Evidence={ECO:0000269|PubMed:15557090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22313;
CC Evidence={ECO:0000269|PubMed:15557090};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (hydrolase route): step 2/2. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9C6D2}.
CC -!- INDUCTION: By sulfur starvation. {ECO:0000269|PubMed:15557090}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000305}.
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DR EMBL; AY593959; AAT06025.1; -; mRNA.
DR EMBL; AL606619; CAE02819.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16121.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91547.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ32355.1; -; Genomic_DNA.
DR EMBL; AK067649; BAG90516.1; -; mRNA.
DR RefSeq; XP_015635941.1; XM_015780455.1.
DR AlphaFoldDB; Q7XR61; -.
DR SMR; Q7XR61; -.
DR STRING; 4530.OS04T0669800-01; -.
DR PaxDb; Q7XR61; -.
DR PRIDE; Q7XR61; -.
DR EnsemblPlants; Os04t0669800-01; Os04t0669800-01; Os04g0669800.
DR GeneID; 4337347; -.
DR Gramene; Os04t0669800-01; Os04t0669800-01; Os04g0669800.
DR KEGG; osa:4337347; -.
DR eggNOG; ENOG502QVM3; Eukaryota.
DR HOGENOM; CLU_033681_0_0_1; -.
DR InParanoid; Q7XR61; -.
DR OMA; EMCEITE; -.
DR OrthoDB; 1140159at2759; -.
DR BioCyc; MetaCyc:MON-10424; -.
DR BRENDA; 2.7.1.100; 4460.
DR PlantReactome; R-OSA-1119624; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XR61; OS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IDA:UniProtKB.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR009212; Methylthioribose_kinase.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF031134; MTRK; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR01767; MTRK; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Methionine biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..430
FT /note="Methylthioribose kinase 1"
FT /id="PRO_0000401364"
FT BINDING 52..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 125..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 263..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C6D2"
FT CONFLICT 72
FT /note="Q -> QQ (in Ref. 1; AAT06025)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="G -> A (in Ref. 1; AAT06025)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> V (in Ref. 1; AAT06025)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="C -> R (in Ref. 1; AAT06025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 48413 MW; 6482051E4935090B CRC64;
MAAAAEQQQQ QQQQGFRPLD EASLVAYIKA TPALAARLGG SLDALTIKEV GDGNLNFVYI
VLSDAGSVVI KQALPYIRCV GDSWPMTRER AYFEASALQK HRGLCPDHVP EVYHFDRAMS
LIGMRYIEPP HIILRKGLIA GVEYPLLAEH MADYMAKTLF FTSLLYNSTT DHKKGVAQYC
DNVEMCRLTE QVVFSDPYML AKYNRCTSPF LDNDAAAVRE DAELKLEIAE LKSMFIERAQ
ALLHGDLHTG SIMVTPDSTQ VIDPEFAFYG PMGYDIGAFL GNLILAYFSQ DGHADQANDR
KAYKKWILKT IEDSWNLFHK KFVELWNKHK DGNGEAYLPP IYNSSELLCL AQKKYMTSLF
HDSLGFGSAK MIRRIVGIAH VEDFESIEDA SKRASCERRA LNCAKAILKG RRQFESIGQV
IVHVQSFDRD
