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P39593

- THIM_BACSU

UniProt

P39593 - THIM_BACSU

Protein

Hydroxyethylthiazole kinase

Gene

thiM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).1 PublicationUniRule annotation

    Catalytic activityi

    ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole.1 PublicationUniRule annotation

    Cofactori

    Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451Substrate; via amide nitrogen1 PublicationUniRule annotation
    Binding sitei121 – 1211ATP
    Binding sitei168 – 1681ATP
    Binding sitei195 – 1951Substrate; via amide nitrogen1 PublicationUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. hydroxyethylthiazole kinase activity Source: UniProtKB-HAMAP
    3. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. thiamine biosynthetic process Source: UniProtKB-KW
    2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU38300-MONOMER.
    MetaCyc:BSU38300-MONOMER.
    UniPathwayiUPA00060; UER00139.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyethylthiazole kinaseUniRule annotation (EC:2.7.1.50UniRule annotation)
    Alternative name(s):
    4-methyl-5-beta-hydroxyethylthiazole kinaseUniRule annotation
    Short name:
    TH kinaseUniRule annotation
    Short name:
    Thz kinaseUniRule annotation
    Gene namesi
    Name:thiMUniRule annotation
    Synonyms:thiK, ywbJ
    Ordered Locus Names:BSU38300
    ORF Names:ipa-25d
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU38300. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981C → A: Reduces activity by 60%. 1 Publication
    Mutagenesisi198 – 1981C → D: Increases activity 10-fold. 1 Publication
    Mutagenesisi198 – 1981C → S: Reduces activity by 80%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 272272Hydroxyethylthiazole kinasePRO_0000156927Add
    BLAST

    Proteomic databases

    PaxDbiP39593.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU38300.

    Structurei

    Secondary structure

    1
    272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Beta strandi19 – 235
    Turni26 – 283
    Helixi29 – 3911
    Beta strandi42 – 443
    Turni49 – 513
    Helixi52 – 587
    Beta strandi59 – 657
    Helixi71 – 8616
    Beta strandi91 – 944
    Helixi102 – 11413
    Beta strandi118 – 1225
    Helixi124 – 1307
    Beta strandi133 – 1386
    Helixi148 – 16114
    Beta strandi163 – 1675
    Beta strandi169 – 1757
    Beta strandi180 – 1834
    Helixi188 – 1925
    Helixi196 – 20813
    Helixi214 – 23623
    Turni237 – 2393
    Helixi241 – 25414
    Helixi257 – 2637
    Beta strandi266 – 2694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C3QX-ray2.00A/B/C1-272[»]
    1EKKX-ray2.00A/B1-272[»]
    1EKQX-ray1.50A/B1-272[»]
    1ESJX-ray1.80A/B/C1-272[»]
    1ESQX-ray2.50A/B/C1-272[»]
    ProteinModelPortaliP39593.
    SMRiP39593. Positions 1-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39593.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Thz kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2145.
    HOGENOMiHOG000114352.
    KOiK00878.
    OMAiQTFTANV.
    OrthoDBiEOG628F8M.
    PhylomeDBiP39593.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    HAMAPiMF_00228. Thz_kinase.
    InterProiIPR000417. Hyethyz_kinase.
    IPR029056. Ribokinase-like.
    [Graphical view]
    PfamiPF02110. HK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000513. Thz_kinase. 1 hit.
    PRINTSiPR01099. HYETHTZKNASE.
    SUPFAMiSSF53613. SSF53613. 1 hit.
    TIGRFAMsiTIGR00694. thiM. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P39593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDAQSAAKCL TAVRRHSPLV HSITNNVVTN FTANGLLALG ASPVMAYAKE    50
    EVADMAKIAG ALVLNIGTLS KESVEAMIIA GKSANEHGVP VILDPVGAGA 100
    TPFRTESARD IIREVRLAAI RGNAAEIAHT VGVTDWLIKG VDAGEGGGDI 150
    IRLAQQAAQK LNTVIAITGE VDVIADTSHV YTLHNGHKLL TKVTGAGCLL 200
    TSVVGAFCAV EENPLFAAIA AISSYGVAAQ LAAQQTADKG PGSFQIELLN 250
    KLSTVTEQDV QEWATIERVT VS 272
    Length:272
    Mass (Da):28,213
    Last modified:February 1, 1995 - v1
    Checksum:i868DDDC0B03DCEAF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73124 Genomic DNA. Translation: CAA51581.1.
    AL009126 Genomic DNA. Translation: CAB15856.1.
    PIRiS39680.
    RefSeqiNP_391709.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15856; CAB15856; BSU38300.
    GeneIDi938519.
    KEGGibsu:BSU38300.
    PATRICi18979706. VBIBacSub10457_4015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73124 Genomic DNA. Translation: CAA51581.1 .
    AL009126 Genomic DNA. Translation: CAB15856.1 .
    PIRi S39680.
    RefSeqi NP_391709.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3Q X-ray 2.00 A/B/C 1-272 [» ]
    1EKK X-ray 2.00 A/B 1-272 [» ]
    1EKQ X-ray 1.50 A/B 1-272 [» ]
    1ESJ X-ray 1.80 A/B/C 1-272 [» ]
    1ESQ X-ray 2.50 A/B/C 1-272 [» ]
    ProteinModelPortali P39593.
    SMRi P39593. Positions 1-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU38300.

    Proteomic databases

    PaxDbi P39593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15856 ; CAB15856 ; BSU38300 .
    GeneIDi 938519.
    KEGGi bsu:BSU38300.
    PATRICi 18979706. VBIBacSub10457_4015.

    Organism-specific databases

    GenoListi BSU38300. [Micado ]

    Phylogenomic databases

    eggNOGi COG2145.
    HOGENOMi HOG000114352.
    KOi K00878.
    OMAi QTFTANV.
    OrthoDBi EOG628F8M.
    PhylomeDBi P39593.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00139 .
    BioCyci BSUB:BSU38300-MONOMER.
    MetaCyc:BSU38300-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39593.

    Family and domain databases

    Gene3Di 3.40.1190.20. 1 hit.
    HAMAPi MF_00228. Thz_kinase.
    InterProi IPR000417. Hyethyz_kinase.
    IPR029056. Ribokinase-like.
    [Graphical view ]
    Pfami PF02110. HK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000513. Thz_kinase. 1 hit.
    PRINTSi PR01099. HYETHTZKNASE.
    SUPFAMi SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00694. thiM. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "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.
    3. "Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis."
      Zhang Y., Taylor S.V., Chiu H.-J., Begley T.P.
      J. Bacteriol. 179:3030-3035(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    4. "Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution."
      Campobasso N., Mathews I.I., Begley T.P., Ealick S.E.
      Biochemistry 39:7868-7877(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, COFACTOR, SUBUNIT, MUTAGENESIS OF CYS-198.

    Entry informationi

    Entry nameiTHIM_BACSU
    AccessioniPrimary (citable) accession number: P39593
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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

    External Data

    Dasty 3