MTK2_ORYSJ
ID MTK2_ORYSJ Reviewed; 427 AA.
AC Q7XR60;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methylthioribose kinase 2;
DE Short=MTR kinase 2;
DE Short=OsMTK2;
DE EC=2.7.1.100;
GN Name=MTK2; OrderedLocusNames=Os04g0669900, LOC_Os04g57410;
GN ORFNames=OsJ_16566, OSJNBa0043A12.25;
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=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 [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=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).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000250}.
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 -!- 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.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000305}.
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DR EMBL; AL606619; CAE02820.1; -; Genomic_DNA.
DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000141; EAZ32356.1; -; Genomic_DNA.
DR RefSeq; XP_015633665.1; XM_015778179.1.
DR AlphaFoldDB; Q7XR60; -.
DR SMR; Q7XR60; -.
DR STRING; 4530.OS04T0669900-00; -.
DR PaxDb; Q7XR60; -.
DR PRIDE; Q7XR60; -.
DR GeneID; 107276080; -.
DR KEGG; osa:107276080; -.
DR eggNOG; ENOG502QVM3; Eukaryota.
DR HOGENOM; CLU_033681_0_0_1; -.
DR InParanoid; Q7XR60; -.
DR OrthoDB; 1140159at2759; -.
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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Methionine biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..427
FT /note="Methylthioribose kinase 2"
FT /id="PRO_0000401365"
FT BINDING 49..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 48228 MW; 561ABC2E1C192A38 CRC64;
MAAAAAEQQQ QGFRPLDEAS LVAYIKATPA LAARLGGRLD ALTIKEVGDG NLNFVYIVLS
DAGSLVIKQA LPYIRLVGDS WPMSRERAYF EASALQKHRA LCPDHVPEVY HFDRAMSLIG
MRYIEPPHII LRKGLVAGVE YPLLAEHMAD YMAKTLFFTS LLYNSTTDHK KGVAQYCDNV
EMSRLTEQVV FSDPYRVAKY NRCTSPFLDN DAAAVREDAE LKLEIAELKS MFIERAQAFL
HGDLHTSSIM VTPDSTQVID PEFAFYGPMG YDIGAFLGNL ILAYFSQDGH ADQANDRKAY
KKWILKTIED SWNFFHKKFV ELWNKHKDGN GEAYLPPIYN SSELLSLVQK KYMTSLFHDS
LGFGSAKMIR RIVGIAHVED FESIEDASKR ASCERRALNC AKAILKGRRQ FESIEQVIVH
VQSFDRD
