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Q8FTH8

- THIED_COREF

UniProt

Q8FTH8 - THIED_COREF

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Protein

Thiamine biosynthesis multifunctional protein ThiED

Gene

thiED

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.By similarity

Catalytic activityi

2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.
ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine.

Cofactori

Mg2+By similarityNote: Binds 1 Mg(2+) ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691HMP-PPBy similarity
Metal bindingi70 – 701MagnesiumBy similarity
Metal bindingi88 – 881MagnesiumBy similarity
Binding sitei107 – 1071HMP-PPBy similarity
Binding sitei143 – 1431HMP-PPBy similarity
Binding sitei174 – 1741THZ-P; via amide nitrogenBy similarity
Binding sitei263 – 2631HydroxymethylpyrimidineBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydroxymethylpyrimidine kinase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. phosphomethylpyrimidine kinase activity Source: UniProtKB-EC
  5. thiamine-phosphate diphosphorylase activity Source: UniProtKB-EC

GO - Biological processi

  1. thiamine biosynthetic process Source: UniProtKB-KW
  2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00060; UER00138.
UPA00060; UER00141.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine biosynthesis multifunctional protein ThiED
Including the following 2 domains:
Thiamine-phosphate synthase (EC:2.5.1.3)
Short name:
TMP-PPase
Short name:
TP synthase
Short name:
TPS
Alternative name(s):
Thiamine-phosphate pyrophosphorylase
Short name:
TMP pyrophosphorylase
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 namesi
Name:thiED
Ordered Locus Names:CE1591
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Thiamine biosynthesis multifunctional protein ThiEDPRO_0000192038Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.CE1591.

Structurei

3D structure databases

ProteinModelPortaliQ8FTH8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 210210Thiamine-phosphate synthaseAdd
BLAST
Regioni37 – 415HMP-PP bindingBy similarity
Regioni140 – 1423THZ-P bindingBy similarity
Regioni194 – 1952THZ-P bindingBy similarity
Regioni226 – 481256Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseAdd
BLAST
Regioni527 – 739213Thiaminase-2Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the thiamine-phosphate synthase family.Curated
In the central section; belongs to the ThiD family.Curated
In the C-terminal section; belongs to the thiaminase-2 family.Curated

Phylogenomic databases

HOGENOMiHOG000225275.
KOiK14153.
OMAiRHELEFF.
OrthoDBiEOG6XWV53.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPiMF_00097. TMP_synthase.
InterProiIPR013785. Aldolase_TIM.
IPR016084. Haem_Oase-like_multi-hlx.
IPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
IPR004305. Thiaminase-2/PQQC.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamiPF08543. Phos_pyr_kin. 1 hit.
PF03070. TENA_THI-4. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMiSSF48613. SSF48613. 1 hit.
SSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
TIGR00693. thiE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8FTH8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE
60 70 80 90 100
HAMELKRVCD RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG
110 120 130 140 150
HLMIGLTIET MDQLETVIAD CTRAGIALPD VVGLGPVQAT DTKPDAPQAV
160 170 180 190 200
GVDGVAAMAK VARAHGIASV AIGGVGLANA ADLARTGVDG LCVVSAIMAA
210 220 230 240 250
PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ ADLKSIAAAG
260 270 280 290 300
GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML
310 320 330 340 350
GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV
360 370 380 390 400
VDVITPNIPE LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG
410 420 430 440 450
PRADNAVVYP DGSVHMVANP RVDTTNSHGT GCSLSAALAT RMGAGHPVDK
460 470 480 490 500
ALDWATRWLN EALRGADALQ VGSGSGPVDH FAVTRRLLRA ADATPWPHLR
510 520 530 540 550
MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG EILDSGFIRG
560 570 580 590 600
LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA
610 620 630 640 650
ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA
660 670 680 690 700
AAVLPCYWLY AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV
710 720 730
EAAMAGAGPD QQRVAAQTYL SACVHEREFF DQATRQGWN
Length:739
Mass (Da):77,744
Last modified:March 1, 2003 - v1
Checksum:iD6631B0553929077
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18401.1.
RefSeqiNP_738201.1. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiBAC18401; BAC18401; BAC18401.
GeneIDi1034064.
KEGGicef:CE1591.
PATRICi21489321. VBICorEff9312_1583.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18401.1 .
RefSeqi NP_738201.1. NC_004369.1.

3D structure databases

ProteinModelPortali Q8FTH8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE1591.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC18401 ; BAC18401 ; BAC18401 .
GeneIDi 1034064.
KEGGi cef:CE1591.
PATRICi 21489321. VBICorEff9312_1583.

Phylogenomic databases

HOGENOMi HOG000225275.
KOi K14153.
OMAi RHELEFF.
OrthoDBi EOG6XWV53.

Enzyme and pathway databases

UniPathwayi UPA00060 ; UER00138 .
UPA00060 ; UER00141 .

Family and domain databases

Gene3Di 1.20.910.10. 1 hit.
3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPi MF_00097. TMP_synthase.
InterProi IPR013785. Aldolase_TIM.
IPR016084. Haem_Oase-like_multi-hlx.
IPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
IPR004305. Thiaminase-2/PQQC.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view ]
Pfami PF08543. Phos_pyr_kin. 1 hit.
PF03070. TENA_THI-4. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view ]
SUPFAMi SSF48613. SSF48613. 1 hit.
SSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsi TIGR00097. HMP-P_kinase. 1 hit.
TIGR00693. thiE. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTHIED_COREF
AccessioniPrimary (citable) accession number: Q8FTH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There is also a ThiE protein in this bacteria (AC Q8FP55).

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3