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Protein

Thiazole synthase

Gene

thiG

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

Functioni

Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H2S.1 Publication

Catalytic activityi

1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O.1 Publication

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei98Schiff-base intermediate with DXP1
Binding sitei159DXP; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciBSUB:BSU11690-MONOMER.
MetaCyc:BSU11690-MONOMER.
BRENDAi2.8.1.10. 658.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiazole synthase (EC:2.8.1.101 Publication)
Gene namesi
Name:thiG
Synonyms:yjbT
Ordered Locus Names:BSU11690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98K → A: No activity; no imine formation with DXP. 1 Publication1
Mutagenesisi100E → A: Activity reduced 38-fold. 1 Publication1
Mutagenesisi184D → A: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001627881 – 256Thiazole synthaseAdd BLAST256

Proteomic databases

PaxDbiO31618.

Interactioni

Subunit structurei

Homotetramer. Forms heterodimers with either ThiH or ThiS.1 Publication

Protein-protein interaction databases

IntActiO31618. 2 interactors.
MINTiMINT-8365876.
STRINGi224308.Bsubs1_010100006461.

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi9 – 12Combined sources4
Beta strandi15 – 18Combined sources4
Helixi25 – 35Combined sources11
Beta strandi38 – 43Combined sources6
Beta strandi44 – 46Combined sources3
Helixi57 – 60Combined sources4
Helixi63 – 65Combined sources3
Beta strandi66 – 71Combined sources6
Helixi78 – 90Combined sources13
Beta strandi95 – 99Combined sources5
Turni105 – 107Combined sources3
Helixi112 – 124Combined sources13
Beta strandi129 – 133Combined sources5
Helixi137 – 145Combined sources9
Beta strandi151 – 153Combined sources3
Beta strandi155 – 157Combined sources3
Helixi167 – 176Combined sources10
Beta strandi181 – 185Combined sources5
Helixi190 – 198Combined sources9
Beta strandi202 – 207Combined sources6
Helixi208 – 211Combined sources4
Beta strandi213 – 215Combined sources3
Helixi216 – 236Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TYGX-ray3.15A/C3-255[»]
1XM3X-ray1.80A/B/C/D1-255[»]
ProteinModelPortaliO31618.
SMRiO31618.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31618.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 186DXP binding2
Regioni207 – 208DXP binding2

Sequence similaritiesi

Belongs to the ThiG family.Curated

Phylogenomic databases

eggNOGiENOG4105CA8. Bacteria.
COG2022. LUCA.
HOGENOMiHOG000248049.
InParanoidiO31618.
KOiK03149.
OMAiAQYPSPA.
PhylomeDBiO31618.

Family and domain databases

CDDicd04728. ThiG. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00443. ThiG. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR008867. ThiG.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLTIGGKS FQSRLLLGTG KYPSFDIQKE AVAVSESDIL TFAVRRMNIF
60 70 80 90 100
EASQPNFLEQ LDLSKYTLLP NTAGASTAEE AVRIARLAKA SGLCDMIKVE
110 120 130 140 150
VIGCSRSLLP DPVETLKASE QLLEEGFIVL PYTSDDVVLA RKLEELGVHA
160 170 180 190 200
IMPGASPIGS GQGILNPLNL SFIIEQAKVP VIVDAGIGSP KDAAYAMELG
210 220 230 240 250
ADGVLLNTAV SGADDPVKMA RAMKLAVEAG RLSYEAGRIP LKQYGTASSP

GEGLPV
Length:256
Mass (Da):27,022
Last modified:January 1, 1998 - v1
Checksum:i39256F75262F97E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13026.1.
PIRiD69845.
RefSeqiNP_389051.1. NC_000964.3.
WP_010886483.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13026; CAB13026; BSU11690.
GeneIDi936422.
KEGGibsu:BSU11690.
PATRICi18974055. VBIBacSub10457_1221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13026.1.
PIRiD69845.
RefSeqiNP_389051.1. NC_000964.3.
WP_010886483.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TYGX-ray3.15A/C3-255[»]
1XM3X-ray1.80A/B/C/D1-255[»]
ProteinModelPortaliO31618.
SMRiO31618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31618. 2 interactors.
MINTiMINT-8365876.
STRINGi224308.Bsubs1_010100006461.

Proteomic databases

PaxDbiO31618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13026; CAB13026; BSU11690.
GeneIDi936422.
KEGGibsu:BSU11690.
PATRICi18974055. VBIBacSub10457_1221.

Phylogenomic databases

eggNOGiENOG4105CA8. Bacteria.
COG2022. LUCA.
HOGENOMiHOG000248049.
InParanoidiO31618.
KOiK03149.
OMAiAQYPSPA.
PhylomeDBiO31618.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciBSUB:BSU11690-MONOMER.
MetaCyc:BSU11690-MONOMER.
BRENDAi2.8.1.10. 658.

Miscellaneous databases

EvolutionaryTraceiO31618.

Family and domain databases

CDDicd04728. ThiG. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00443. ThiG. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR008867. ThiG.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIG_BACSU
AccessioniPrimary (citable) accession number: O31618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 117 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

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.