P71350 (THIE_HAEIN) 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:	HI_0417

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	226 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) 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 Reference 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 – 226	226	Thiamine-phosphate synthase		PRO_0000157016
Regions
	Region	46 – 50	5	HMP-PP binding By similarity
	Region	149 – 151	3	THZ-P binding By similarity
	Region	201 – 202	2	THZ-P binding By similarity
Sites
	Metal binding	84	1	Magnesium By similarity
	Metal binding	103	1	Magnesium By similarity
	Binding site	83	1	HMP-PP By similarity
	Binding site	122	1	HMP-PP By similarity
	Binding site	152	1	HMP-PP By similarity
	Binding site	181	1	THZ-P; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P71350 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: C5EB00DED081EEE7	FASTA	226	24,730
	10 20 30 40 50 60 MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS 70 80 90 100 110 120 AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG 130 140 150 160 170 180 WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG 190 200 210 220 GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Two-dimensional map of the proteome of Haemophilus influenzae." Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., Fountoulakis M. Electrophoresis 21:411-429(2000) [PubMed: 10675023] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22075.1.
PIR	A64152.
RefSeq	NP_438579.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P71350.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949518.
GenomeReviews	Gene locus HI_0417 in contig L42023_GR.
KEGG	hin:HI0417.
NMPDR	fig|71421.1.peg.392.
PATRIC	20189387. VBIHaeInf48452_0437.
TIGR	HI_0417.
Phylogenomic databases
HOGENOM	HBG754477.
OMA	FIINDDV.
PhylomeDB	P71350.
ProtClustDB	PRK00043.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0417-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_HAEIN

Accession

Primary (citable) accession number: P71350

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program