Q186F8 (THIE_CLOD6) 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:	CD630_16010

Organism

Clostridium difficile (strain 630) [Complete proteome] [HAMAP]

Taxonomic identifier

272563 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Clostridium difficile

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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) By similarity. HAMAP-Rule MF_00097
Catalytic activity	2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. HAMAP-Rule MF_00097
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.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete 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 – 210	210	Thiamine-phosphate synthase HAMAP-Rule MF_00097		PRO_0000336386
Regions
	Region	43 – 47	5	HMP-PP binding By similarity
	Region	140 – 142	3	THZ-P binding By similarity
	Region	190 – 191	2	THZ-P binding By similarity
Sites
	Metal binding	76	1	Magnesium By similarity
	Metal binding	95	1	Magnesium By similarity
	Binding site	75	1	HMP-PP By similarity
	Binding site	114	1	HMP-PP By similarity
	Binding site	143	1	HMP-PP By similarity
	Binding site	170	1	THZ-P; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q186F8 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: F50956BE21E60D7E	FASTA	210	23,414
	10 20 30 40 50 60 MIDKESLKKC LKLYLVTDSE MLKGRDFYKC LEDAISSGIT TVQLREKNAS GREFLRKAMK 70 80 90 100 110 120 LREITKRYGV KFIINDRVDI ALICDADGVH VGQSDIDVRE VRKLIGNNKI LGVSARTLEE 130 140 150 160 170 180 AICAKNDGAD YLGVGSIFTT STKLDAKSAS FETVKEIKEK VDMPFVLIGG INLDNIDKLK 190 200 210 CLESDGYAII SAILKAEDIS KEVEKWTLKI

References

[1]

"The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. , Cronin A., Davis P., Dowd L., Fraser A., Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J. Nat. Genet. 38:779-786(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180355 Genomic DNA. Translation: CAJ68466.1.
RefSeq	YP_001088102.1. NC_009089.1.
3D structure databases
ProteinModelPortal	Q186F8.
ModBase	Search...
Protein-protein interaction databases
STRING	272563.CD1601.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ68466; CAJ68466; CD630_16010.
GeneID	4913386.
KEGG	cdf:CD630_16010.
PATRIC	19441581. VBICloDif38397_1678.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0352.
HOGENOM	HOG000155781.
KO	K00788.
OMA	VDIALIC.
ProtClustDB	CLSK2534956.
Enzyme and pathway databases
BioCyc	CDIF272563:GJFE-1777-MONOMER.
UniPathway	UPA00060; UER00141.
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_CLOD6

Accession

Primary (citable) accession number: Q186F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	July 25, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program