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) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

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-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. HAMAP-Rule 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-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 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 – 226	226	Thiamine-phosphate synthase HAMAP-Rule MF_00097		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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

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...
Protein-protein interaction databases
STRING	71421.HI0417.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22075; AAC22075; HI_0417.
GeneID	949518.
KEGG	hin:HI0417.
PATRIC	20189387. VBIHaeInf48452_0437.
Phylogenomic databases
eggNOG	COG0352.
KO	K00788.
OMA	LFFVNDR.
ProtClustDB	PRK00043.
Enzyme and pathway databases
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_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:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program