P39593 (THIM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	thiM
Synonyms:	thiK, ywbJ
Ordered Locus Names:	BSU38300
ORF Names:	ipa-25d

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. HAMAP-Rule MF_00228
Cofactor	Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. HAMAP-Rule MF_00228
Subunit structure	Homotrimer. Ref.4
Sequence similarities	Belongs to the Thz kinase family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP hydroxyethylthiazole kinase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 272

272

Hydroxyethylthiazole kinase HAMAP-Rule MF_00228

PRO_0000156927

Sites

Binding site

45

1

Substrate; via amide nitrogen

Binding site

121

1

ATP

Binding site

168

1

ATP

Binding site

195

1

Substrate; via amide nitrogen

Experimental info

Mutagenesis

198

1

C → A: Reduces activity by 60%. Ref.4

Mutagenesis

198

1

C → D: Increases activity 10-fold. Ref.4

Mutagenesis

198

1

C → S: Reduces activity by 80%. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

272

Helix Strand Turn

Details...

Helix

3 – 16

14

Beta strand

19 – 23

5

Turn

26 – 28

3

Helix

29 – 39

11

Beta strand

42 – 44

3

Turn

49 – 51

3

Helix

52 – 58

7

Beta strand

59 – 65

7

Helix

71 – 86

16

Beta strand

91 – 94

4

Helix

102 – 114

13

Beta strand

118 – 122

5

Helix

124 – 130

7

Beta strand

133 – 138

6

Helix

148 – 161

14

Beta strand

163 – 167

5

Beta strand

169 – 175

7

Beta strand

180 – 183

4

Helix

188 – 192

5

Helix

196 – 208

13

Helix

214 – 236

23

Turn

237 – 239

3

Helix

241 – 254

14

Helix

257 – 263

7

Beta strand

266 – 269

4

Sequences

	Sequence		Length	Mass (Da)
	P39593 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 868DDDC0B03DCEAF	FASTA	272	28,213
	10 20 30 40 50 60 MDAQSAAKCL TAVRRHSPLV HSITNNVVTN FTANGLLALG ASPVMAYAKE EVADMAKIAG 70 80 90 100 110 120 ALVLNIGTLS KESVEAMIIA GKSANEHGVP VILDPVGAGA TPFRTESARD IIREVRLAAI 130 140 150 160 170 180 RGNAAEIAHT VGVTDWLIKG VDAGEGGGDI IRLAQQAAQK LNTVIAITGE VDVIADTSHV 190 200 210 220 230 240 YTLHNGHKLL TKVTGAGCLL TSVVGAFCAV EENPLFAAIA AISSYGVAAQ LAAQQTADKG 250 260 270 PGSFQIELLN KLSTVTEQDV QEWATIERVT VS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees." Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A. Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73124 Genomic DNA. Translation: CAA51581.1.
AL009126 Genomic DNA. Translation: CAB15856.1.

PIR

S39680.

RefSeq

NP_391709.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P39593.

SMR

P39593. Positions 1-272.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU38300.

Proteomic databases

PaxDb

P39593.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15856; CAB15856; BSU38300.

GeneID

938519.

KEGG

bsu:BSU38300.

PATRIC

18979706. VBIBacSub10457_4015.

Organism-specific databases

GenoList

BSU38300. [Micado]

Phylogenomic databases

eggNOG

COG2145.

HOGENOM

HOG000114352.

KO

K00878.

OMA

SPVMAHA.

ProtClustDB

PRK09355.

Enzyme and pathway databases

BioCyc

BSUB:BSU38300-MONOMER.
MetaCyc:BSU38300-MONOMER.

UniPathway

UPA00060; UER00139.

Family and domain databases

HAMAP

MF_00228. Thz_kinase.

InterPro

IPR000417. Hyethyz_kinase.
IPR026012. Hyethyz_kinase/Th_synth.
[Graphical view]

PANTHER

PTHR20857:SF14. PTHR20857:SF14. 1 hit.

Pfam

PF02110. HK. 1 hit.
[Graphical view]

PIRSF

PIRSF000513. Thz_kinase. 1 hit.

PRINTS

PR01099. HYETHTZKNASE.

TIGRFAMs

TIGR00694. thiM. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P39593.

Entry information

Entry name

THIM_BACSU

Accession

Primary (citable) accession number: P39593

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program