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A8FUV3 (THIG_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiazole synthase

EC=2.8.1.10
Gene names
Name:thiG
Ordered Locus Names:Ssed_2017
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00443

Catalytic activity

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. HAMAP-Rule MF_00443

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00443

Subunit structure

Homotetramer. Forms heterodimers with either ThiH or ThiS By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00443.

Sequence similarities

Belongs to the ThiG family.

Ontologies

Keywords
   Biological processThiamine biosynthesis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processthiamine diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-iminoacetate synthase activity

Inferred from electronic annotation. Source: InterPro

sulfurtransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Thiazole synthase HAMAP-Rule MF_00443
PRO_1000080880

Regions

Region182 – 1832DXP binding By similarity
Region204 – 2052DXP binding By similarity

Sites

Active site951Schiff-base intermediate with DXP By similarity
Binding site1561DXP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FUV3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: D63C92FD77A6EFE7

FASTA25427,054
        10         20         30         40         50         60 
MLKIAEHEFN SRLFTGTGKF SSANLMLEAI QASQSQLVTM AMKRLDLSSG SDEILLPLQQ 

        70         80         90        100        110        120 
SGIKLLPNTS GARNAKEAVF AAELAREVLN TNWVKLEIHP DPKYLMPDPI ETLAAAKTLC 

       130        140        150        160        170        180 
DKGFVVLPYV HADPVLCRRL EEVGCAAVMP LASPIGSNQG LATETFLKII IEQASVPVVV 

       190        200        210        220        230        240 
DAGIGTPSQA THAMELGADA VLVNTAIASS RDPIAMARCF SQAVETGRAA YRAGLGQVSV 

       250 
RAEHTSPLTG FLNE 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV36626.1.
RefSeqYP_001473754.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FUV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_2017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV36626; ABV36626; Ssed_2017.
GeneID5613839.
KEGGsse:Ssed_2017.
PATRIC23561542. VBISheSed62411_2145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2022.
HOGENOMHOG000248049.
KOK03149.
OMATAGCFTA.
OrthoDBEOG6KMBD9.

Enzyme and pathway databases

BioCycSSED425104:GH7Q-2081-MONOMER.
UniPathwayUPA00060.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00443. ThiG.
InterProIPR013785. Aldolase_TIM.
IPR008867. ThiG.
[Graphical view]
PfamPF05690. ThiG. 1 hit.
[Graphical view]
SUPFAMSSF110399. SSF110399. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIG_SHESH
AccessionPrimary (citable) accession number: A8FUV3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways