MTNK_ECO45
ID MTNK_ECO45 Reviewed; 419 AA.
AC B7MMH5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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, ECO:0000269|PubMed:31950558};
GN Name=mtnK {ECO:0000255|HAMAP-Rule:MF_01683, ECO:0000303|PubMed:31950558};
GN OrderedLocusNames=ECS88_4901 {ECO:0000312|EMBL:CAR06047.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25922 / DSM 1103 / NCIB 12210 / ExPEC;
RX PubMed=31950558; DOI=10.1111/mmi.14459;
RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA Tabita F.R.;
RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT products that is widespread in bacteria, including pathogenic Escherichia
RT coli.";
RL Mol. Microbiol. 113:923-937(2020).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate (PubMed:31950558). Also catalyzes the
CC phosphorylation of 5-deoxyribose to 5-deoxyribose-1-phosphate
CC (PubMed:31950558). Part of a bifunctional DHAP-shunt salvage pathway
CC for SAM by-products (PubMed:31950558). {ECO:0000269|PubMed:31950558}.
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 ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22313;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-D-ribose + ATP = 5-deoxy-alpha-D-ribose 1-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:61288, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58749, ChEBI:CHEBI:149540,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61289;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=186 uM for 5-methythioribose {ECO:0000269|PubMed:31950558};
CC KM=25 uM for 5-deoxyribose {ECO:0000269|PubMed:31950558};
CC KM=2265 uM for S-ribosyl-L-homocysteine
CC {ECO:0000269|PubMed:31950558};
CC KM=18181 uM for ribose {ECO:0000269|PubMed:31950558};
CC KM=83 uM for ATP (in the presence of 5-deoxyribose)
CC {ECO:0000269|PubMed:31950558};
CC Note=kcat is 10.6 sec(-1) with 5-methythioribose as substrate. kcat
CC is 16.1 sec(-1) with 5-deoxyribose as substrate. kcat is 5.4 sec(-1)
CC with S-ribosyl-L-homocysteine as substrate. kcat is 11.6 sec(-1) with
CC ribose as substrate. kcat is 14.1 with ATP as substrate.
CC {ECO:0000269|PubMed:31950558};
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, ECO:0000269|PubMed:31950558}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01683}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene precludes growth of the
CC strain with 5-deoxyribose. {ECO:0000269|PubMed:31950558}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01683}.
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DR EMBL; CU928161; CAR06047.1; -; Genomic_DNA.
DR RefSeq; WP_000132327.1; NC_011742.1.
DR AlphaFoldDB; B7MMH5; -.
DR SMR; B7MMH5; -.
DR EnsemblBacteria; CAR06047; CAR06047; ECS88_4901.
DR KEGG; ecz:ECS88_4901; -.
DR HOGENOM; CLU_033681_0_0_6; -.
DR OMA; EMCEITE; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000000747; Chromosome.
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 HAMAP; MF_01683; Salvage_MtnK; 1.
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; Transferase.
FT CHAIN 1..419
FT /note="Methylthioribose kinase"
FT /id="PRO_0000450353"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01683"
SQ SEQUENCE 419 AA; 47658 MW; A16AE19E6F05B3EE CRC64;
MTDSIPSGYK PLTCDTLPGY LSSRLTPSCE PGGLPEEWKV SEVGDGNLNM VFIVEGTHKT
IIVKQALPWL RAGGEGWPLS LSRAGFEYNV LCQEAKYAGH TLIPQVYFYD PEMALFAMEY
LTPHVILRKE LINGKKFPKL AEDIGRFLAQ TLFNTSDIGM SAEQKKALTA EFALNHELCK
ITEDLIFTEP YYNAERNNWT SPELDDAVHK AWADVEMIQV AMRYKYKFMT EAQALLHGDL
HSGSIMVTDT DTKVIDPEFG FMGPMAFDIG NYIGNLLLAY FSRPGWDANE QRRADYQEWL
LQQIVQTWSV FTREFRQLWD NKTQGDAWST EMYQQNRAAL EDAQDQFFAT LLEDSLVNAG
MEMNRRIIGF AGVAELKQIE NTELRAGCER RALTMARDLI VNARQFKNMD SVIQSAKVK
