P30137 (THIE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamine-phosphate synthase
Short name=TP synthase
Short name=TPS
EC=2.5.1.3

Alternative name(s):
Thiamine-phosphate pyrophosphorylase
Short name=TMP pyrophosphorylase
Short name=TMP-PPase

Gene names

Name:	thiE
Ordered Locus Names:	b3993, JW3957

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Ref.5 Ref.7
Catalytic activity	2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. Ref.5
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. HAMAP-Rule MF_00097
Sequence similarities	Belongs to the thiamine-phosphate synthase family.
Biophysicochemical properties	Kinetic parameters: KM=1 µM for HMP-PP Ref.5 KM=2 µM for THZ-P
Mass spectrometry	Molecular mass is 23014.8 Da from positions 1 - 211. Determined by ESI. Ref.6

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamine-phosphate diphosphorylase 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 – 211	211	Thiamine-phosphate synthase HAMAP-Rule MF_00097		PRO_0000157010
Regions
	Region	37 – 41	5	HMP-PP binding By similarity
	Region	134 – 136	3	THZ-P binding By similarity
	Region	186 – 187	2	THZ-P binding By similarity
Sites
	Metal binding	70	1	Magnesium By similarity
	Metal binding	89	1	Magnesium By similarity
	Binding site	69	1	HMP-PP By similarity
	Binding site	108	1	HMP-PP By similarity
	Binding site	137	1	HMP-PP By similarity
	Binding site	166	1	THZ-P; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30137 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: C731953E46BC33E1	FASTA	211	23,015
	10 20 30 40 50 60 MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR 70 80 90 100 110 120 RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA 130 140 150 160 170 180 ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV 190 200 210 GSIAVVSAIT QAADWRLATA QLLEIAGVGD E

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Biosynthesis of thiamin I: the function of the thiE gene product." Backstrom A.D., Austin R., McMordie S., Begley T.P. J. Am. Chem. Soc. 117:2351-2352(1995) Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
[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] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[7]	"A genetic screen for the identification of thiamin metabolic genes." Lawhorn B.G., Gerdes S.Y., Begley T.P. J. Biol. Chem. 279:43555-43559(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THIAMINE METABOLISM. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M88701 Genomic DNA. Translation: AAB95617.1. U00006 Genomic DNA. Translation: AAC43091.1. U00096 Genomic DNA. Translation: AAC76967.1. AP009048 Genomic DNA. Translation: BAE77326.1.
PIR	S35118.
RefSeq	NP_418421.1. NC_000913.2. YP_491467.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P30137.
SMR	P30137. Positions 20-202.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10983N.
IntAct	P30137. 4 interactions.
MINT	MINT-1247897.
STRING	511145.b3993.
2D gel databases
SWISS-2DPAGE	P30137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76967; AAC76967; b3993. BAE77326; BAE77326; BAE77326.
GeneID	12930339. 948491.
KEGG	ecj:Y75_p3203. eco:b3993.
PATRIC	32123509. VBIEscCol129921_4107.
Organism-specific databases
EchoBASE	EB1545.
EcoGene	EG11586. thiE.
Phylogenomic databases
eggNOG	COG0352.
HOGENOM	HOG000155781.
KO	K00788.
OMA	YWRAAIV.
ProtClustDB	PRK03512.
Enzyme and pathway databases
BioCyc	EcoCyc:THIE-MONOMER. ECOL316407:JW3957-MONOMER. MetaCyc:THIE-MONOMER.
UniPathway	UPA00060; UER00141.
Gene expression databases
Genevestigator	P30137.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00097. TMP_synthase.
InterPro	IPR013785. Aldolase_TIM. IPR022998. ThiaminP_synth_SF. IPR003733. TMP_synthase. [Graphical view]
Pfam	PF02581. TMP-TENI. 1 hit. [Graphical view]
SUPFAM	SSF51391. TMP_synthase. 1 hit.
TIGRFAMs	TIGR00693. thiE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIE_ECOLI

Accession

Primary (citable) accession number: P30137
Secondary accession number(s): Q2M8T0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program