ID H3R9J1_PANSE Unreviewed; 399 AA.
AC H3R9J1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Methylthioribose kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE Short=MTR kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE EC=2.7.1.100 {ECO:0000256|HAMAP-Rule:MF_01683};
GN Name=mtnK {ECO:0000256|HAMAP-Rule:MF_01683};
GN ORFNames=CKS_0305 {ECO:0000313|EMBL:EHU01854.1}, DSJ_19590
GN {ECO:0000313|EMBL:ARF51303.1};
OS Pantoea stewartii subsp. stewartii DC283.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHU01854.1, ECO:0000313|Proteomes:UP000005050};
RN [1] {ECO:0000313|EMBL:EHU01854.1, ECO:0000313|Proteomes:UP000005050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:EHU01854.1,
RC ECO:0000313|Proteomes:UP000005050};
RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA Wang X., Yang F., von Bodman S.B.;
RT "The genetic and structural basis of two distinct terminal side branch
RT residues in stewartan and amylovoran exopolysaccharides and their potential
RT role in host adaptation.";
RL Mol. Microbiol. 83:195-207(2012).
RN [2] {ECO:0000313|EMBL:EHU01854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DC283 {ECO:0000313|EMBL:EHU01854.1};
RA Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA Weinstock G.M.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ARF51303.1, ECO:0000313|Proteomes:UP000192380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:ARF51303.1,
RC ECO:0000313|Proteomes:UP000192380};
RA Duong D.A., Stevens A.M., Jensen R.V.;
RT "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT Corn Pathogen.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01683}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01683}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000256|ARBA:ARBA00010165, ECO:0000256|HAMAP-Rule:MF_01683}.
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DR EMBL; CP017581; ARF51303.1; -; Genomic_DNA.
DR EMBL; AHIE01000002; EHU01854.1; -; Genomic_DNA.
DR RefSeq; WP_006118041.1; NZ_CP017581.1.
DR AlphaFoldDB; H3R9J1; -.
DR STRING; 660596.DSJ_19590; -.
DR KEGG; pstw:DSJ_19590; -.
DR PATRIC; fig|660596.6.peg.539; -.
DR eggNOG; COG4857; Bacteria.
DR OrthoDB; 9777791at2; -.
DR UniPathway; UPA00904; UER00872.
DR Proteomes; UP000005050; Unassembled WGS sequence.
DR Proteomes; UP000192380; 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 {ECO:0000256|HAMAP-Rule:MF_01683};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:EHU01854.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_01683}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:EHU01854.1}.
FT DOMAIN 31..265
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 111..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 246..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01683"
SQ SEQUENCE 399 AA; 44755 MW; 33AC55C05381C785 CRC64;
MSQYRTFTAA DAVEYAKQFG GLEDPSVLRS AEEIGDGNLN QVFKIYDDQG NSRIVVKQAL
PYVRCVGESW PLTLDRARIE AQTLVEHYKY CPQHTVNVTH YDADLAVMIM EDLSSHRIWR
SELVKGAYYP EAPRQLGEYL AQTLFHTSDF ILHPHVKKAE VARFINPELC EITEDLFFND
PYTDHVRNSY PEALEPLVAS LRTDEALRIA VAGLKHRFFS HAEALLHGDI HSGSIFVADG
SLKAIDAEFG YFGPMGFDVG TALGNLLINY CGLPGLLPPR EAADAREQRL SDVHDVWQTF
ETRFLALAES KTQDVAMAYP GYAQAFLRKV WADTIGYCGT ELIRRTVGMS HVADMKLIRD
EEMRTDCIRN AITLGRTLIL AAGHVDDVDA LIARIRQAG
//
