ID MTNK_PECAS Reviewed; 400 AA.
AC Q6D1H0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Methylthioribose kinase {ECO:0000255|HAMAP-Rule:MF_01683};
DE Short=MTR kinase {ECO:0000255|HAMAP-Rule:MF_01683};
DE EC=2.7.1.100 {ECO:0000255|HAMAP-Rule:MF_01683};
GN Name=mtnK {ECO:0000255|HAMAP-Rule:MF_01683}; OrderedLocusNames=ECA3476;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01683}.
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:0000255|HAMAP-Rule:MF_01683};
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:0000255|HAMAP-
CC Rule:MF_01683}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01683}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01683}.
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DR EMBL; BX950851; CAG76375.1; -; Genomic_DNA.
DR RefSeq; WP_011094983.1; NC_004547.2.
DR AlphaFoldDB; Q6D1H0; -.
DR SMR; Q6D1H0; -.
DR STRING; 218491.ECA3476; -.
DR GeneID; 57210145; -.
DR KEGG; eca:ECA3476; -.
DR PATRIC; fig|218491.5.peg.3518; -.
DR eggNOG; COG4857; Bacteria.
DR HOGENOM; CLU_033681_0_0_6; -.
DR OrthoDB; 9777791at2; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 1.
DR HAMAP; MF_01683; Salvage_MtnK; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR009212; Methylthioribose_kinase.
DR NCBIfam; TIGR01767; MTRK; 1.
DR PANTHER; PTHR34273; METHYLTHIORIBOSE KINASE; 1.
DR PANTHER; PTHR34273:SF2; METHYLTHIORIBOSE KINASE; 1.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF031134; MTRK; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Methionine biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="Methylthioribose kinase"
FT /id="PRO_0000357341"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 111..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 246..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ SEQUENCE 400 AA; 44489 MW; 61E097E9A0AAF803 CRC64;
MSLYRTFTAD DAVEYARQYG GVSQPQTLVT AEEIGDGNLN LVFKIKDEAG ISRVIVKQAL
PYVRCVGESW PLTLDRARIE AETLLTHARF CPQHTVTVLY HDPELAVMVQ EDLSDHRIWR
SELVRGADYP QAAAQLGEYL AQTLFHTSDF YQHPHEKKAA VSQFTNPELC EITEDLFFTD
PYIDHERNQF DAALTPDVQT LRDDRALKLA VAGLKHRFLS KAEALLHGDI HSGSIFVAEG
RLKVIDAEFG FYGPMGFDIG TAIGNLLLNY CGLPGLLAPR EAAAGRERRL EDIRTLWQTF
SARFLALSES DCREPALAES GYAALFLQQV WLDAIGFCGT ELIRRTIGLA HVVDLDSIQE
TDARLACQRH VLSLGRTLVL AAPHIADVDA LLARVRQSGA
//
