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Protein

Methylthioribose kinase

Gene

mtnK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.1 Publication

Catalytic activityi

ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate.

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 2 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
  2. Methylthioribose kinase (mtnK)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441ATP
Binding sitei61 – 611ATP
Binding sitei233 – 2331Substrate
Binding sitei340 – 3401Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi115 – 1173ATP
Nucleotide bindingi250 – 2523ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU13560-MONOMER.
BRENDAi2.7.1.100. 658.
SABIO-RKO31663.
UniPathwayiUPA00904; UER00872.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribose kinase (EC:2.7.1.100)
Short name:
MTR kinase
Gene namesi
Name:mtnK
Synonyms:ykrT
Ordered Locus Names:BSU13560
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Methylthioribose kinasePRO_0000162915Add
BLAST

Proteomic databases

PaxDbiO31663.

Expressioni

Inductioni

By starvation.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiO31663. 1 interaction.
MINTiMINT-8365168.
STRINGi224308.Bsubs1_010100007516.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2310Combined sources
Beta strandi34 – 374Combined sources
Beta strandi40 – 5011Combined sources
Beta strandi52 – 554Combined sources
Beta strandi57 – 637Combined sources
Helixi66 – 683Combined sources
Helixi80 – 9213Combined sources
Helixi96 – 983Combined sources
Beta strandi102 – 1065Combined sources
Turni107 – 1104Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi120 – 1223Combined sources
Helixi123 – 1286Combined sources
Helixi136 – 15015Combined sources
Turni153 – 1553Combined sources
Helixi158 – 16710Combined sources
Helixi171 – 18010Combined sources
Turni181 – 1833Combined sources
Helixi184 – 1863Combined sources
Helixi196 – 1983Combined sources
Helixi199 – 2068Combined sources
Helixi209 – 22416Combined sources
Beta strandi228 – 2303Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 27617Combined sources
Helixi279 – 2824Combined sources
Helixi283 – 30725Combined sources
Turni311 – 3144Combined sources
Helixi318 – 34326Combined sources
Beta strandi344 – 3463Combined sources
Helixi349 – 3524Combined sources
Helixi357 – 37721Combined sources
Turni378 – 3803Combined sources
Helixi384 – 39411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLCX-ray2.00A/B1-397[»]
2PU8X-ray2.10A/B1-397[»]
2PUIX-ray2.20A/B1-397[»]
2PULX-ray2.00A/B1-397[»]
2PUNX-ray2.30A/B1-397[»]
2PUPX-ray2.60A/B1-397[»]
ProteinModelPortaliO31663.
SMRiO31663. Positions 5-396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31663.

Family & Domainsi

Sequence similaritiesi

Belongs to the methylthioribose kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105CT5. Bacteria.
COG4857. LUCA.
HOGENOMiHOG000082744.
InParanoidiO31663.
OMAiEMCEITE.
OrthoDBiEOG635877.

Family and domain databases

HAMAPiMF_01683. Salvage_MtnK.
InterProiIPR002575. Aminoglycoside_PTrfase.
IPR011009. Kinase-like_dom.
IPR009212. Methylthioribose_kinase.
[Graphical view]
PfamiPF01636. APH. 1 hit.
[Graphical view]
PIRSFiPIRSF031134. MTRK. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR01767. MTRK. 1 hit.

Sequencei

Sequence statusi: Complete.

O31663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVTKTPLYE TLNESSAVAL AVKLGLFPSK STLTCQEIGD GNLNYVFHIY
60 70 80 90 100
DQEHDRALII KQAVPYAKVV GESWPLTIDR ARIESSALIR QGEHVPHLVP
110 120 130 140 150
RVFYSDTEMA VTVMEDLSHL KIARKGLIEG ENYPHLSQHI GEFLGKTLFY
160 170 180 190 200
SSDYALEPKV KKQLVKQFTN PELCDITERL VFTDPFFDHD TNDFEEELRP
210 220 230 240 250
FVEKLWNNDS VKIEAAKLKK SFLTSAETLI HGDLHTGSIF ASEHETKVID
260 270 280 290 300
PEFAFYGPIG FDVGQFIANL FLNALSRDGA DREPLYEHVN QVWETFEETF
310 320 330 340 350
SEAWQKDSLD VYANIDGYLT DTLSHIFEEA IGFAGCELIR RTIGLAHVAD
360 370 380 390
LDTIVPFDKR IGRKRLALET GTAFIEKRSE FKTITDVIEL FKLLVKE
Length:397
Mass (Da):45,085
Last modified:October 24, 2003 - v2
Checksum:iE5862F8D8492189C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13229.2.
PIRiD69863.
RefSeqiWP_003244973.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13229; CAB13229; BSU13560.
PATRICi18974480. VBIBacSub10457_1432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13229.2.
PIRiD69863.
RefSeqiWP_003244973.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLCX-ray2.00A/B1-397[»]
2PU8X-ray2.10A/B1-397[»]
2PUIX-ray2.20A/B1-397[»]
2PULX-ray2.00A/B1-397[»]
2PUNX-ray2.30A/B1-397[»]
2PUPX-ray2.60A/B1-397[»]
ProteinModelPortaliO31663.
SMRiO31663. Positions 5-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31663. 1 interaction.
MINTiMINT-8365168.
STRINGi224308.Bsubs1_010100007516.

Proteomic databases

PaxDbiO31663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13229; CAB13229; BSU13560.
PATRICi18974480. VBIBacSub10457_1432.

Phylogenomic databases

eggNOGiENOG4105CT5. Bacteria.
COG4857. LUCA.
HOGENOMiHOG000082744.
InParanoidiO31663.
OMAiEMCEITE.
OrthoDBiEOG635877.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00872.
BioCyciBSUB:BSU13560-MONOMER.
BRENDAi2.7.1.100. 658.
SABIO-RKO31663.

Miscellaneous databases

EvolutionaryTraceiO31663.

Family and domain databases

HAMAPiMF_01683. Salvage_MtnK.
InterProiIPR002575. Aminoglycoside_PTrfase.
IPR011009. Kinase-like_dom.
IPR009212. Methylthioribose_kinase.
[Graphical view]
PfamiPF01636. APH. 1 hit.
[Graphical view]
PIRSFiPIRSF031134. MTRK. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR01767. MTRK. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis."
    Sekowska A., Mulard L., Krogh S., Tse J.K.S., Danchin A.
    BMC Microbiol. 1:15-15(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, REANALYSIS OF N-TERMINUS.
  3. "The methionine salvage pathway in Bacillus subtilis."
    Sekowska A., Danchin A.
    BMC Microbiol. 2:8-8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "ADP-2Ho as a phasing tool for nucleotide-containing proteins."
    Ku S.-Y., Smith G.D., Howell P.L.
    Acta Crystallogr. D 63:493-499(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP-2HO, SUBUNIT.
  5. "Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding."
    Ku S.Y., Yip P., Cornell K.A., Riscoe M.K., Behr J.B., Guillerm G., Howell P.L.
    J. Biol. Chem. 282:22195-22206(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ADENOSYL NUCLEOTIDES AND SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiMTNK_BACSU
AccessioniPrimary (citable) accession number: O31663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: February 17, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.