Q9WZP7 (THIDN_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional thiamine biosynthesis protein ThiDN

Including the following 2 domains:

1. Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
   EC=2.7.1.49
   EC=2.7.4.7
   Alternative name(s):
   Hydroxymethylpyrimidine kinase
   Short name=HMP kinase
   Hydroxymethylpyrimidine phosphate kinase
   Short name=HMP-P kinase
   Short name=HMP-phosphate kinase
   Short name=HMPP kinase
2. Thiamine-phosphate synthase ThiN
   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:	thiDN
Ordered Locus Names:	TM_0790

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P By similarity. Ref.2 Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Ref.2
Catalytic activity	ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. Ref.2 ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Ref.2 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. Ref.2
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole. Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Sequence similarities	In the N-terminal section; belongs to the ThiD family. In the C-terminal section; belongs to the ThiN family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydroxymethylpyrimidine kinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro phosphomethylpyrimidine kinase activity Inferred from electronic annotation. Source: EC 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 – 398	398	Bifunctional thiamine biosynthesis protein ThiDN		PRO_0000415381
Regions
	Region	1 – 216	216	Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
	Region	217 – 398	182	Thiamine-phosphate synthase
Sites
	Binding site	40	1	Hydroxymethylpyrimidine/phosphomethylpyrimidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WZP7 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: DCE6977F471BF649	FASTA	398	45,392
	10 20 30 40 50 60 MVLVVAGFDP SGGAGIIQDV KVLSALGVKT HAVISALTVQ NENRVFSVNF RDWEEMRKEI 70 80 90 100 110 120 EVLTPPRVIK VGLSAPETVK RLREMFPDSA IVWNVVLESS SGFGFQDPEE VKKFVEYADY 130 140 150 160 170 180 VILNSEEAKK LGEYNNFIVT GGHEKGNTVK VKYRDFVFEI PRVPGEFHGT GCAFSSAVSG 190 200 210 220 230 240 FLAMSYPVEE AIRSAMELLK KILERSSGVV ETEKLLRDWY RYDTLNTLDE ILPEFLEIGH 250 260 270 280 290 300 LTVPEVGQNV SYALPWAKNE FEVGKFPGRI RLKEGKAVAV SCASFKDRSH TARMAVTMMR 310 320 330 340 350 360 YHPHMRCVVN VRYEREYVER AKKRGLKVFH YDRSKEPKEV QEKEGQSMVW MIEQAIAELK 370 380 390 SPPDVIYDEG WWGKEAMIRV FGRNPKEVLE KIKLMVRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Systematic discovery of analogous enzymes in thiamin biosynthesis." Morett E., Korbel J.O., Rajan E., Saab-Rincon G., Olvera L., Olvera M., Schmidt S., Snel B., Bork P. Nat. Biotechnol. 21:790-795(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A THIAMINE-PHOSPHATE SYNTHASE VIA ITS C-TERMINAL DOMAIN, CATALYTIC ACTIVITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35872.1.
PIR	G72333.
RefSeq	NP_228599.1. NC_000853.1.
3D structure databases
HSSP	HSSP built from PDB template 1JXH based on UniProtKB P55882.
ProteinModelPortal	Q9WZP7.
ModBase	Search...
Protein-protein interaction databases
STRING	243274.TM0790.
Protocols and materials databases
DNASU	898458.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD35872; AAD35872; TM_0790.
GeneID	898458.
KEGG	tma:TM0790.
PATRIC	23936500. VBITheMar51294_0802.
Phylogenomic databases
KO	K00941.
OMA	YDRREEP.
ProtClustDB	CLSK875375.
Enzyme and pathway databases
UniPathway	UPA00060; UER00141.
Family and domain databases
Gene3D	3.40.225.10. 1 hit.
InterPro	IPR001303. Aldolase_II/adducin_N. IPR013749. HMP-P_kinase-1. IPR019293. ThiN. [Graphical view]
Pfam	PF10120. Aldolase_2. 1 hit. PF08543. Phos_pyr_kin. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THIDN_THEMA

Accession

Primary (citable) accession number: Q9WZP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program