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Protein

Thiazole synthase

Gene

thiG

Organism
Maricaulis maris (strain MCS10)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

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.UniRule annotation

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
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 sitei110Schiff-base intermediate with DXPUniRule annotation1
Binding sitei171DXP; via amide nitrogenUniRule annotation1

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

UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiazole synthaseUniRule annotation (EC:2.8.1.10UniRule annotation)
Gene namesi
Name:thiGUniRule annotation
Ordered Locus Names:Mmar10_1269
OrganismiMaricaulis maris (strain MCS10)
Taxonomic identifieri394221 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis
Proteomesi
  • UP000001964 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002061381 – 267Thiazole synthaseAdd BLAST267

Interactioni

Subunit structurei

Homotetramer. Forms heterodimers with either ThiH or ThiS.UniRule annotation

Protein-protein interaction databases

STRINGi394221.Mmar10_1269.

Structurei

3D structure databases

ProteinModelPortaliQ0AQ76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 198DXP bindingUniRule annotation2
Regioni219 – 220DXP bindingUniRule annotation2

Sequence similaritiesi

Belongs to the ThiG family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CA8. Bacteria.
COG2022. LUCA.
HOGENOMiHOG000248049.
KOiK03149.
OMAiAQYPSPA.
OrthoDBiPOG091H01K9.

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.

Q0AQ76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDAVTMDTA FEDKPLVVAG RTFTSRLIIG TGKYKTYAQN AQALEASGAE
60 70 80 90 100
MITVAIRRVN LSNPDEPRLV DFISPDDYTF LPNTAGCFTG EDAVRTLRLA
110 120 130 140 150
REAGGWNLVK LEVLSDPKHL YPDMAETLRA AELLIKDGFD VMVYCSDDPV
160 170 180 190 200
YARKLEEIGC CAIMPLGAPI GSGLGIQNPV NIRLIIEQTK VPVIVDAGVG
210 220 230 240 250
TASDATVAME LGCDGVLMNT AIAEAKDPIR MARAMRHAVI AGRESYLAGR
260
MPKKRYADPS SPLSGLI
Length:267
Mass (Da):28,793
Last modified:October 17, 2006 - v1
Checksum:i678AB0579FFA8C96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000449 Genomic DNA. Translation: ABI65561.1.
RefSeqiWP_011643208.1. NC_008347.1.

Genome annotation databases

EnsemblBacteriaiABI65561; ABI65561; Mmar10_1269.
KEGGimmr:Mmar10_1269.
PATRICi22450612. VBIMarMar77530_1299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000449 Genomic DNA. Translation: ABI65561.1.
RefSeqiWP_011643208.1. NC_008347.1.

3D structure databases

ProteinModelPortaliQ0AQ76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi394221.Mmar10_1269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI65561; ABI65561; Mmar10_1269.
KEGGimmr:Mmar10_1269.
PATRICi22450612. VBIMarMar77530_1299.

Phylogenomic databases

eggNOGiENOG4105CA8. Bacteria.
COG2022. LUCA.
HOGENOMiHOG000248049.
KOiK03149.
OMAiAQYPSPA.
OrthoDBiPOG091H01K9.

Enzyme and pathway databases

UniPathwayiUPA00060.

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_MARMM
AccessioniPrimary (citable) accession number: Q0AQ76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 75 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.