MTK_ARATH
ID MTK_ARATH Reviewed; 420 AA.
AC Q9C6D2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Methylthioribose kinase {ECO:0000303|PubMed:15557090};
DE Short=AtMTK {ECO:0000303|PubMed:15557090};
DE Short=MTR kinase {ECO:0000303|PubMed:15557090};
DE EC=2.7.1.100 {ECO:0000269|PubMed:17961230};
GN Name=MTK {ECO:0000303|PubMed:15557090};
GN OrderedLocusNames=At1g49820 {ECO:0000312|Araport:AT1G49820};
GN ORFNames=F10F5.1 {ECO:0000312|EMBL:AAG51775.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17144895; DOI=10.1111/j.1365-313x.2006.02942.x;
RA Buerstenbinder K., Rzewuski G., Wirtz M., Hell R., Sauter M.;
RT "The role of methionine recycling for ethylene synthesis in Arabidopsis.";
RL Plant J. 49:238-249(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBUNIT.
RX PubMed=17961230; DOI=10.1186/1472-6807-7-70;
RA Ku S.Y., Cornell K.A., Howell P.L.;
RT "Structure of Arabidopsis thaliana 5-methylthioribose kinase reveals a more
RT occluded active site than its bacterial homolog.";
RL BMC Struct. Biol. 7:70-70(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate in the methionine cycle. Contributes to
CC the maintenance of AdoMet homeostasis and is required to sustain high
CC rates of ethylene synthesis. {ECO:0000269|PubMed:17144895,
CC ECO:0000269|PubMed:17961230}.
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:17961230};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:17961230};
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 {ECO:0000269|PubMed:17961230}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17961230}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition (PubMed:15557090). Not able to grow with methylthioadenosine
CC (MTA) as unique source of sulfur (PubMed:15557090). Imbalanced AdoMet
CC homeostasis in sulfur-limiting conditions associated with a retarded
CC growth (PubMed:17144895). {ECO:0000269|PubMed:15557090,
CC ECO:0000269|PubMed:17144895}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000305}.
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DR EMBL; AC079674; AAG51775.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32480.1; -; Genomic_DNA.
DR EMBL; AY057512; AAL09753.1; -; mRNA.
DR EMBL; AY090315; AAL90976.1; -; mRNA.
DR PIR; A96535; A96535.
DR RefSeq; NP_564555.1; NM_103869.4.
DR PDB; 2PYW; X-ray; 1.90 A; A/B=1-420.
DR PDBsum; 2PYW; -.
DR AlphaFoldDB; Q9C6D2; -.
DR SMR; Q9C6D2; -.
DR BioGRID; 26630; 6.
DR STRING; 3702.AT1G49820.1; -.
DR iPTMnet; Q9C6D2; -.
DR PaxDb; Q9C6D2; -.
DR PRIDE; Q9C6D2; -.
DR ProteomicsDB; 250983; -.
DR EnsemblPlants; AT1G49820.1; AT1G49820.1; AT1G49820.
DR GeneID; 841405; -.
DR Gramene; AT1G49820.1; AT1G49820.1; AT1G49820.
DR KEGG; ath:AT1G49820; -.
DR Araport; AT1G49820; -.
DR TAIR; locus:2007253; AT1G49820.
DR eggNOG; ENOG502QVM3; Eukaryota.
DR HOGENOM; CLU_033681_0_0_1; -.
DR InParanoid; Q9C6D2; -.
DR OMA; EMCEITE; -.
DR OrthoDB; 1140159at2759; -.
DR PhylomeDB; Q9C6D2; -.
DR BioCyc; ARA:AT1G49820-MON; -.
DR BRENDA; 2.7.1.100; 399.
DR UniPathway; UPA00904; UER00872.
DR EvolutionaryTrace; Q9C6D2; -.
DR PRO; PR:Q9C6D2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6D2; baseline and differential.
DR Genevisible; Q9C6D2; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IDA:UniProtKB.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; TAS:TAIR.
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 3D-structure; Acetylation; Amino-acid biosynthesis; ATP-binding; Kinase;
KW Methionine biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..420
FT /note="Methylthioribose kinase"
FT /id="PRO_0000401363"
FT BINDING 44..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 117..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 255..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17961230,
FT ECO:0007744|PDB:2PYW"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 293..320
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:2PYW"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 337..368
FT /evidence="ECO:0007829|PDB:2PYW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 382..402
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2PYW"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:2PYW"
SQ SEQUENCE 420 AA; 48071 MW; 92809E787ED28B69 CRC64;
MSFEEFTPLN EKSLVDYIKS TPALSSKIGA DKSDDDLVIK EVGDGNLNFV FIVVGSSGSL
VIKQALPYIR CIGESWPMTK ERAYFEATTL RKHGNLSPDH VPEVYHFDRT MALIGMRYLE
PPHIILRKGL IAGIEYPFLA DHMSDYMAKT LFFTSLLYHD TTEHRRAVTE FCGNVELCRL
TEQVVFSDPY RVSTFNRWTS PYLDDDAKAV REDSALKLEI AELKSMFCER AQALIHGDLH
TGSVMVTQDS TQVIDPEFSF YGPMGFDIGA YLGNLILAFF AQDGHATQEN DRKEYKQWIL
RTIEQTWNLF NKRFIALWDQ NKDGPGEAYL ADIYNNTEVL KFVQENYMRN LLHDSLGFGA
AKMIRRIVGV AHVEDFESIE EDKRRAICER SALEFAKMLL KERRKFKSIG EVVSAIQQQS
