Reviewed, UniProtKB/Swiss-Prot Q8U192 (THIE_PYRFU)

Names and origin

Protein names

Recommended name:
    Thiamine-phosphate pyrophosphorylase
      Short name=TMP pyrophosphorylase
      Short name=TMP-PPase
    EC=2.5.1.3
Alternative name(s):
    Thiamine-phosphate synthase

Gene names

Name:	thiE
Ordered Locus Names:	PF1334

Organism

Pyrococcus furiosus [Complete proteome] [HAMAP]

Taxonomic identifier

2261 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	207 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 TMP-PPase family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	thiamin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamin-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 – 207

207

Thiamine-phosphate pyrophosphorylase HAMAP MF_00097

PRO_0000157074

Sites

Metal binding

69

1

Magnesium By similarity

Metal binding

88

1

Magnesium By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

207

Helix Strand Turn

Details...

Helix

3 – 6

4

Beta strand

8 – 12

5

Turn

15 – 17

3

Helix

20 – 29

10

Beta strand

33 – 37

5

Helix

44 – 60

17

Beta strand

64 – 69

6

Helix

71 – 77

7

Beta strand

80 – 84

5

Helix

91 – 97

7

Beta strand

101 – 109

9

Helix

110 – 119

10

Beta strand

122 – 127

6

Helix

142 – 152

11

Beta strand

157 – 162

6

Turn

165 – 167

3

Helix

168 – 172

5

Turn

173 – 175

3

Beta strand

177 – 182

6

Helix

183 – 186

4

Beta strand

188 – 190

3

Helix

191 – 206

16

Sequences

	Sequence		Length	Mass (Da)
	Q8U192-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 7776F777009AE858	FASTA	207	22,590
	10 20 30 40 50 60 MNLRNKLKLY VITDRRLKPE VESVREALEG GATAIQMRIK NAPTREMYEI GKTLRQLTRE 70 80 90 100 110 120 YDALFFVDDR VDVALAVDAD GVQLGPEDMP IEVAKEIAPN LIIGASVYSL EEALEAEKKG 130 140 150 160 170 180 ADYLGAGSVF PTKTKEDARV IGLEGLRKIV ESVKIPVVAI GGINKDNARE VLKTGVDGIA 190 200 VISAVMGAED VRKATEELRK IVEEVLG

References

[1]	"The complete sequence of the Pyrococcus furiosus genome." Weiss R.B., Dunn D.M., Robb F.T., Brown J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE009950 Genomic DNA. Translation: AAL81458.1.

RefSeq

NP_579063.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XI3	X-ray	1.70	A/B	2-207	[»]

ModBase

Search...

Genome annotation databases

GeneID

1469209.

GenomeReviews

Gene locus PF1334 in contig AE009950_GR.

KEGG

pfu:PF1334.

NMPDR

fig|186497.1.peg.1380.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG754477.

OMA

IMGSNNC.

Enzyme and pathway databases

BRENDA

2.5.1.3. 321.

Family and domain databases

HAMAP

MF_00097. TMP-PPase.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR003733. TMP_synthase.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF02581. TMP-TENI. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00693. thiE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

THIE_PYRFU

Accession

Primary (citable) accession number: Q8U192

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)