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P39593

- THIM_BACSU

UniProt

P39593 - THIM_BACSU

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Protein
Hydroxyethylthiazole kinase
Gene
thiM, thiK, ywbJ, BSU38300, ipa-25d
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole.UniRule 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.

Pathwayi

Sites

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

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
Complete GO annotation...

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 kinase (EC:2.7.1.50)
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinase
Short name:
TH kinase
Short name:
Thz kinase
Gene namesi
Name:thiM
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 kinaseUniRule annotation
PRO_0000156927Add
BLAST

Proteomic databases

PaxDbiP39593.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU38300.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP39593.

Family & Domainsi

Sequence similaritiesi

Belongs to the Thz kinase family.

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

« Hide 'large scale' publications
  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: CHARACTERIZATION.
  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, HOMOTRIMERIZATION, 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: July 9, 2014
This is version 120 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

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