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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-adenylate-[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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Schiff-base intermediate with DXP
Binding sitei159 – 1591DXP; via amide nitrogen

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:2.8.1.10)
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 981K → A: No activity; no imine formation with DXP. 1 Publication
Mutagenesisi100 – 1001E → A: Activity reduced 38-fold. 1 Publication
Mutagenesisi184 – 1841D → A: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Thiazole synthasePRO_0000162788Add
BLAST

Proteomic databases

PaxDbiO31618.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi9 – 124Combined sources
Beta strandi15 – 184Combined sources
Helixi25 – 3511Combined sources
Beta strandi38 – 436Combined sources
Beta strandi44 – 463Combined sources
Helixi57 – 604Combined sources
Helixi63 – 653Combined sources
Beta strandi66 – 716Combined sources
Helixi78 – 9013Combined sources
Beta strandi95 – 995Combined sources
Turni105 – 1073Combined sources
Helixi112 – 12413Combined sources
Beta strandi129 – 1335Combined sources
Helixi137 – 1459Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi155 – 1573Combined sources
Helixi167 – 17610Combined sources
Beta strandi181 – 1855Combined sources
Helixi190 – 1989Combined sources
Beta strandi202 – 2076Combined sources
Helixi208 – 2114Combined sources
Beta strandi213 – 2153Combined sources
Helixi216 – 23621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYGX-ray3.15A/C3-255[»]
1XM3X-ray1.80A/B/C/D1-255[»]
ProteinModelPortaliO31618.
SMRiO31618. Positions 2-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31618.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1862DXP binding
Regioni207 – 2082DXP binding

Sequence similaritiesi

Belongs to the ThiG family.Curated

Phylogenomic databases

eggNOGiENOG4105CA8. Bacteria.
COG2022. LUCA.
HOGENOMiHOG000248049.
InParanoidiO31618.
KOiK03149.
OMAiAQYPSPA.
OrthoDBiEOG6KMBD9.
PhylomeDBiO31618.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00443. ThiG.
InterProiIPR013785. Aldolase_TIM.
IPR008867. ThiG.
[Graphical view]
SUPFAMiSSF110399. SSF110399. 1 hit.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYGX-ray3.15A/C3-255[»]
1XM3X-ray1.80A/B/C/D1-255[»]
ProteinModelPortaliO31618.
SMRiO31618. Positions 2-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31618. 2 interactions.
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.
OrthoDBiEOG6KMBD9.
PhylomeDBiO31618.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO31618.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00443. ThiG.
InterProiIPR013785. Aldolase_TIM.
IPR008867. ThiG.
[Graphical view]
SUPFAMiSSF110399. SSF110399. 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. "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)."
    Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W., Begley T.P.
    Biochemistry 42:12430-12438(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: 168 / CU1065.
  3. "The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS."
    Dorrestein P.C., Zhai H., McLafferty F.W., Begley T.P.
    Chem. Biol. 11:1373-1381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTION MECHANISM.
  4. "The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase."
    Dorrestein P.C., Zhai H., Taylor S.V., McLafferty F.W., Begley T.P.
    J. Am. Chem. Soc. 126:3091-3096(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTION MECHANISM, MUTAGENESIS OF LYS-98, ROLE OF LYS-98 IN SCHIFF BASE FORMATION WITH DXP.
    Strain: 168 / CU1065.
  5. "Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction."
    Hazra A., Chatterjee A., Begley T.P.
    J. Am. Chem. Soc. 131:3225-3229(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTION PRODUCTS, REACTION MECHANISM.
  6. "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex."
    Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., McLafferty F.W., Begley T.P., Ealick S.E.
    Biochemistry 43:11647-11657(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 3-255 IN COMPLEX WITH SULFUR CARRIER PROTEIN THIS AND PHOSPHATE, MUTAGENESIS OF GLU-100 AND ASP-184, SUBUNIT, REACTION MECHANISM.
  7. "Crystal structure of northeast structural genomics target sr156."
    Northeast structural genomics consortium (NESG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-255.

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: February 17, 2016
This is version 113 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.