Q8FTH8 (THIED_COREF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamine biosynthesis multifunctional protein ThiED

Including the following 2 domains:

1. Thiamine-phosphate synthase
   Short name=TMP-PPase
   Short name=TP synthase
   Short name=TPS
   EC=2.5.1.3
   Alternative name(s):
   Thiamine-phosphate pyrophosphorylase
   Short name=TMP pyrophosphorylase
2. 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

Gene names

Name:	thiED
Ordered Locus Names:	CE1591

Organism

Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]

Taxonomic identifier

196164 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium efficiens

Protein attributes

Sequence length	739 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-Rule MF_00097 Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P 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 ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. HAMAP-Rule MF_00097 ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. HAMAP-Rule MF_00097
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00097
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3. HAMAP-Rule MF_00097 Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Miscellaneous	There is also a ThiE protein in this bacteria (AC Q8FP55). HAMAP-Rule MF_00097
Sequence similarities	In the N-terminal section; belongs to the thiamine-phosphate synthase family. In the central section; belongs to the ThiD family. In the C-terminal section; belongs to the thiaminase-2 family.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Multifunctional enzyme
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: UniProtKB-KW 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 – 739	739	Thiamine biosynthesis multifunctional protein ThiED HAMAP-Rule MF_00097		PRO_0000192038
Regions
	Region	1 – 210	210	Thiamine-phosphate synthase HAMAP-Rule MF_00097
	Region	37 – 41	5	HMP-PP binding By similarity
	Region	140 – 142	3	THZ-P binding By similarity
	Region	194 – 195	2	THZ-P binding By similarity
	Region	226 – 481	256	Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase HAMAP-Rule MF_00097
	Region	527 – 739	213	Thiaminase-2 HAMAP-Rule MF_00097
Sites
	Metal binding	70	1	Magnesium By similarity
	Metal binding	88	1	Magnesium By similarity
	Binding site	69	1	HMP-PP By similarity
	Binding site	107	1	HMP-PP By similarity
	Binding site	143	1	HMP-PP By similarity
	Binding site	174	1	THZ-P; via amide nitrogen By similarity
	Binding site	263	1	Hydroxymethylpyrimidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FTH8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D6631B0553929077	FASTA	739	77,744
	10 20 30 40 50 60 MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE HAMELKRVCD 70 80 90 100 110 120 RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG HLMIGLTIET MDQLETVIAD 130 140 150 160 170 180 CTRAGIALPD VVGLGPVQAT DTKPDAPQAV GVDGVAAMAK VARAHGIASV AIGGVGLANA 190 200 210 220 230 240 ADLARTGVDG LCVVSAIMAA PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ 250 260 270 280 290 300 ADLKSIAAAG GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML 310 320 330 340 350 360 GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV VDVITPNIPE 370 380 390 400 410 420 LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG PRADNAVVYP DGSVHMVANP 430 440 450 460 470 480 RVDTTNSHGT GCSLSAALAT RMGAGHPVDK ALDWATRWLN EALRGADALQ VGSGSGPVDH 490 500 510 520 530 540 FAVTRRLLRA ADATPWPHLR MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG 550 560 570 580 590 600 EILDSGFIRG LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA 610 620 630 640 650 660 ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA AAVLPCYWLY 670 680 690 700 710 720 AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV EAAMAGAGPD QQRVAAQTYL 730 SACVHEREFF DQATRQGWN

References

[1]

"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000035 Genomic DNA. Translation: BAC18401.1.
RefSeq	NP_738201.1. NC_004369.1.
3D structure databases
ProteinModelPortal	Q8FTH8.
ModBase	Search...
Protein-protein interaction databases
STRING	196164.CE1591.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC18401; BAC18401; BAC18401.
GeneID	1034064.
KEGG	cef:CE1591.
PATRIC	21489321. VBICorEff9312_1583.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000225275.
KO	K14153.
OMA	TIVIVKG.
ProtClustDB	PRK09517.
Enzyme and pathway databases
UniPathway	UPA00060; UER00138. UPA00060; UER00141.
Family and domain databases
Gene3D	1.20.910.10. 1 hit. 3.20.20.70. 1 hit.
HAMAP	MF_00097. TMP_synthase. Fused.
InterPro	IPR013785. Aldolase_TIM. IPR016084. Haem_Oase-like_multi-hlx. IPR013749. HMP-P_kinase-1. IPR004399. HMP-P_kinase-2. IPR004305. Thiaminase-2/PQQC. IPR022998. ThiaminP_synth_SF. IPR003733. TMP_synthase. [Graphical view]
Pfam	PF08543. Phos_pyr_kin. 1 hit. PF03070. TENA_THI-4. 1 hit. PF02581. TMP-TENI. 1 hit. [Graphical view]
SUPFAM	SSF48613. Heme_oxygenase. 1 hit. SSF51391. TMP_synthase. 1 hit.
TIGRFAMs	TIGR00097. HMP-P_kinase. 1 hit. TIGR00693. thiE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

THIED_COREF

Accession

Primary (citable) accession number: Q8FTH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program