P66918 (THIE_STAAM) 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:	SAV2091

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	213 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 MF_00097
Catalytic activity	2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. HAMAP MF_00097
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00097
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 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: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamine-phosphate diphosphorylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Thiamine-phosphate synthase		PRO_0000157043
Regions
	Region	40 – 44	5	HMP-PP binding By similarity
	Region	139 – 141	3	THZ-P binding By similarity
	Region	191 – 192	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	113	1	HMP-PP By similarity
	Binding site	142	1	HMP-PP By similarity
	Binding site	171	1	THZ-P; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P66918 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 8FEFB39D6EF82F94	FASTA	213	23,399
	10 20 30 40 50 60 MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE 70 80 90 100 110 120 LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY 130 140 150 160 170 180 AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI 190 200 210 VEAGANGISV ISAISKSENI EKTVNRFKDF FNN

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000017 Genomic DNA. Translation: BAB58253.1.
RefSeq	NP_372615.1. NC_002758.2.
3D structure databases
ProteinModelPortal	P66918.
ModBase	Search...
Protein-protein interaction databases
STRING	P66918.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000007385; EBSTAP00000007203; EBSTAG00000007384.
GeneID	1122108.
GenomeReviews	Gene locus SAV2091 in contig BA000017_GR.
KEGG	sav:SAV2091.
PATRIC	19565060. VBIStaAur52173_2165.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0352.
GeneTree	EBGT00050000024447.
HOGENOM	HBG754477.
OMA	FIINDDV.
PhylomeDB	P66918.
ProtClustDB	PRK00043.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV2091-MONOMER.
Family and domain databases
HAMAP	MF_00097. TMP_synthase. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR022998. ThiaminP_synth_SF. IPR003733. TMP_synthase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00788.
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_STAAM

Accession

Primary (citable) accession number: P66918
Secondary accession number(s): Q99SG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program