Q8G2U9 (THIG_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiazole synthase
EC=2.8.1.10

Gene names

Name:	thiG
Ordered Locus Names:	BR0215, BS1330_I0215

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Thiamine biosynthesis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2-iminoacetate synthase activity Inferred from electronic annotation. Source: InterPro sulfurtransferase activity 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 – 256	256	Thiazole synthase HAMAP-Rule MF_00443		PRO_0000162798
Regions
	Region	184 – 185	2	DXP binding By similarity
	Region	206 – 207	2	DXP binding By similarity
Sites
	Active site	96	1	Schiff-base intermediate with DXP By similarity
	Binding site	157	1	DXP; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G2U9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B4BB14EEA3EA18D0	FASTA	256	27,351
	10 20 30 40 50 60 MLEFYGKRFE SRLLLGTAQY PSPSILADAV RASLSRIVTV SLRRESGEAR AGQDFWALIK 70 80 90 100 110 120 ALGVAVLPNT AGCHTPREAI TTAHMAREVF GTNWIKLEVI GDTDTLQPDP FGLVEAARIL 130 140 150 160 170 180 CDESFEVFPY MNDDLIVAER LIEAGCKVLM PWGAPIGSGR GLNNPYALKT MRAHFPDIPL 190 200 210 220 230 240 VVDAGIGVPS HAAAAMELGF DAVLINTAVA KAGDPAAMAR AFALAVEAGR LAYEADPIEA 250 RDMASPSTPL LGKAFL

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29164.1. CP002997 Genomic DNA. Translation: AEM17576.1.
RefSeq	NP_697249.1. NC_004310.3. YP_005615068.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8G2U9.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR0215.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN29164; AAN29164; BR0215. AEM17576; AEM17576; BS1330_I0215.
GeneID	1165873. 12138757.
KEGG	bms:BR0215. bsi:BS1330_I0215.
PATRIC	17788699. VBIBruSui107850_0221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2022.
HOGENOM	HOG000248049.
KO	K03149.
OMA	TAGCFTA.
ProtClustDB	PRK00208.
Enzyme and pathway databases
UniPathway	UPA00060.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00443. ThiG.
InterPro	IPR013785. Aldolase_TIM. IPR008867. ThiG. [Graphical view]
Pfam	PF05690. ThiG. 1 hit. [Graphical view]
SUPFAM	SSF110399. ThiG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIG_BRUSU

Accession

Primary (citable) accession number: Q8G2U9
Secondary accession number(s): G0KBR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program