P30139 (THIG_ECOLI) 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:	b3991, JW5549

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.5
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 MF_00443
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP MF_00443
Subunit structure	Homotetramer. Forms heterodimers with either ThiH or ThiS. Ref.5
Subcellular location	Cytoplasm HAMAP MF_00443.
Sequence similarities	Belongs to the ThiG family.
Mass spectrometry	Molecular mass is 26893.3 Da from positions 1 - 256. Determined by ESI. Ref.5 Molecular mass is 26896.5 Da from positions 1 - 256. Determined by ESI. Ref.6
Sequence caution	The sequence AAC43089.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
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 MF_00443		PRO_0000162815
Regions
	Region	182 – 183	2	DXP binding By similarity
	Region	204 – 205	2	DXP binding By similarity
Sites
	Active site	95	1	Schiff-base intermediate with DXP By similarity
	Binding site	156	1	DXP; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30139 [UniParc]. Last modified August 29, 2001. Version 3. Checksum: 8B0BDEE617104E38	FASTA	256	26,896
	10 20 30 40 50 60 MLRIADKTFD SHLFTGTGKF ASSQLMVEAI RASGSQLVTL AMKRVDLRQH NDAILEPLIA 70 80 90 100 110 120 AGVTLLPNTS GAKTAEEAIF AAHLAREALG TNWLKLEIHP DARWLLPDPI ETLKAAETLV 130 140 150 160 170 180 QQGFVVLPYC GADPVLCKRL EEVGCAAVMP LGAPIGSNQG LETRAMLEII IQQATVPVVV 190 200 210 220 230 240 DAGIGVPSHA AQALEMGADA VLVNTAIAVA DDPVNMAKAF RLAVEAGLLA RQSGPGSRSY 250 FAHATSPLTG FLEASA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12." Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P. J. Bacteriol. 175:982-992(1993) [PubMed: 8432721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex." Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L. FEBS Lett. 539:95-99(2003) [PubMed: 12650933] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7, FUNCTION, MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH THIH.
[6]	"Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry." Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W. Protein Sci. 7:1796-1801(1998) [PubMed: 10082377] [Abstract] Cited for: MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M88701 Genomic DNA. Translation: AAB95621.1. U00006 Genomic DNA. Translation: AAC43089.1. Different initiation. U00096 Genomic DNA. Translation: AAC76965.2. AP009048 Genomic DNA. Translation: BAE77329.1.
PIR	B65206.
RefSeq	NP_418418.2. NC_000913.2.
3D structure databases
ProteinModelPortal	P30139.
SMR	P30139. Positions 1-238.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6868N.
IntAct	P30139. 9 interactions.
MINT	MINT-1289283.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000061; EBESCP00000000061; EBESCG00000000047. EBESCT00000016457; EBESCP00000015748; EBESCG00000015517.
GeneID	948493.
GenomeReviews	Gene locus JW5549 in contig AP009048_GR. Gene locus b3991 in contig U00096_GR.
KEGG	ecj:JW5549. eco:b3991.
PATRIC	32123503. VBIEscCol129921_4104.
Organism-specific databases
EchoBASE	EB1547.
EcoGene	EG11589. thiG.
Phylogenomic databases
eggNOG	COG2022.
GeneTree	EBGT00050000011495.
HOGENOM	HBG296821.
OMA	TAGCFTA.
PhylomeDB	P30139.
ProtClustDB	PRK00208.
Enzyme and pathway databases
BioCyc	EcoCyc:THIG-MONOMER. MetaCyc:THIG-MONOMER.
Gene expression databases
Genevestigator	P30139.
Family and domain databases
HAMAP	MF_00443. ThiG. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR008867. ThiG. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K03149.
Pfam	PF05690. ThiG. 1 hit. [Graphical view]
SUPFAM	SSF110399. ThiG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIG_ECOLI

Accession

Primary (citable) accession number: P30139
Secondary accession number(s): P76779, Q2M8S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	August 29, 2001
Last modified:	January 25, 2012
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program