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Protein

Thiamine-monophosphate kinase

Gene

thiL

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.UniRule annotation1 Publication

Catalytic activityi

ATP + thiamine phosphate = ADP + thiamine diphosphate.UniRule annotation

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes thiamine diphosphate from thiamine phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Thiamine-monophosphate kinase (thiL)
This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine diphosphate from thiamine phosphate, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27Magnesium 31 Publication1
Metal bindingi27Magnesium 4; via carbonyl oxygen1 Publication1
Metal bindingi41Magnesium 41 Publication1
Metal bindingi42Magnesium 1; via carbonyl oxygen1 Publication1
Metal bindingi43Magnesium 11 Publication1
Metal bindingi43Magnesium 21 Publication1
Binding sitei50Substrate1 Publication1
Metal bindingi71Magnesium 21 Publication1
Metal bindingi71Magnesium 31 Publication1
Metal bindingi71Magnesium 41 Publication1
Binding sitei101ATP1 Publication1
Metal bindingi119Magnesium 11 Publication1
Binding sitei142ATP1 Publication1
Metal bindingi207Magnesium 31 Publication1
Binding sitei209ATP1 Publication1
Metal bindingi210Magnesium 51 Publication1
Binding sitei260Substrate1 Publication1
Binding sitei303Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi118 – 119ATP1 Publication2

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.4.16. 396.
UniPathwayiUPA00060; UER00142.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-monophosphate kinaseUniRule annotation (EC:2.7.4.16UniRule annotation)
Short name:
TMP kinaseUniRule annotation
Short name:
Thiamine-phosphate kinaseUniRule annotation
Gene namesi
Name:thiL
Ordered Locus Names:aq_2119
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004155171 – 306Thiamine-monophosphate kinaseAdd BLAST306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34Interchain1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224324.aq_2119.

Structurei

Secondary structure

1306
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi8 – 19Combined sources12
Beta strandi26 – 33Combined sources8
Beta strandi36 – 46Combined sources11
Turni47 – 49Combined sources3
Helixi57 – 74Combined sources18
Beta strandi78 – 88Combined sources11
Helixi94 – 111Combined sources18
Beta strandi114 – 122Combined sources9
Beta strandi127 – 138Combined sources12
Beta strandi150 – 155Combined sources6
Helixi159 – 168Combined sources10
Helixi176 – 186Combined sources11
Helixi192 – 194Combined sources3
Helixi195 – 201Combined sources7
Beta strandi203 – 210Combined sources8
Helixi212 – 223Combined sources12
Beta strandi226 – 229Combined sources4
Helixi231 – 233Combined sources3
Helixi238 – 246Combined sources9
Helixi251 – 257Combined sources7
Beta strandi263 – 268Combined sources6
Helixi270 – 272Combined sources3
Turni275 – 278Combined sources4
Beta strandi279 – 293Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VQVX-ray2.65A/B1-306[»]
3C9RX-ray2.30A/B1-306[»]
3C9SX-ray2.20A/B1-306[»]
3C9TX-ray2.60A/B1-306[»]
3C9UX-ray1.48A/B1-306[»]
ProteinModelPortaliO67883.
SMRiO67883.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67883.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiamine-monophosphate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CG2. Bacteria.
COG0611. LUCA.
HOGENOMiHOG000228428.
InParanoidiO67883.
KOiK00946.
OMAiMTDNSDG.
OrthoDBiPOG091H016U.

Family and domain databases

CDDicd02194. ThiL. 1 hit.
Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_02128. TMP_kinase. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR006283. ThiL.
[Graphical view]
PANTHERiPTHR30270. PTHR30270. 1 hit.
PfamiPF00586. AIRS. 1 hit.
[Graphical view]
PIRSFiPIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR01379. thiL. 1 hit.

Sequencei

Sequence statusi: Complete.

O67883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLKELGEFG LIDLIKKTLE SKVIGDDTAP VEYCSKKLLL TTDVLNEGVH
60 70 80 90 100
FLRSYIPEAV GWKAISVNVS DVIANGGLPK WALISLNLPE DLEVSYVERF
110 120 130 140 150
YIGVKRACEF YKCEVVGGNI SKSEKIGISV FLVGETERFV GRDGARLGDS
160 170 180 190 200
VFVSGTLGDS RAGLELLLME KEEYEPFELA LIQRHLRPTA RIDYVKHIQK
210 220 230 240 250
YANASMDISD GLVADANHLA QRSGVKIEIL SEKLPLSNEL KMYCEKYGKN
260 270 280 290 300
PIEYALFGGE DYQLLFTHPK ERWNPFLDMT EIGRVEEGEG VFVDGKKVEP

KGWKHF
Length:306
Mass (Da):34,413
Last modified:August 1, 1998 - v1
Checksum:iB5E5E63489D9BB32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07848.1.
PIRiG70481.
RefSeqiNP_214452.1. NC_000918.1.
WP_010881388.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07848; AAC07848; aq_2119.
GeneIDi1193872.
KEGGiaae:aq_2119.
PATRICi20961084. VBIAquAeo85532_1635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07848.1.
PIRiG70481.
RefSeqiNP_214452.1. NC_000918.1.
WP_010881388.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VQVX-ray2.65A/B1-306[»]
3C9RX-ray2.30A/B1-306[»]
3C9SX-ray2.20A/B1-306[»]
3C9TX-ray2.60A/B1-306[»]
3C9UX-ray1.48A/B1-306[»]
ProteinModelPortaliO67883.
SMRiO67883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_2119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07848; AAC07848; aq_2119.
GeneIDi1193872.
KEGGiaae:aq_2119.
PATRICi20961084. VBIAquAeo85532_1635.

Phylogenomic databases

eggNOGiENOG4105CG2. Bacteria.
COG0611. LUCA.
HOGENOMiHOG000228428.
InParanoidiO67883.
KOiK00946.
OMAiMTDNSDG.
OrthoDBiPOG091H016U.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00142.
BRENDAi2.7.4.16. 396.

Miscellaneous databases

EvolutionaryTraceiO67883.

Family and domain databases

CDDicd02194. ThiL. 1 hit.
Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_02128. TMP_kinase. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR016188. PurM-like_N.
IPR006283. ThiL.
[Graphical view]
PANTHERiPTHR30270. PTHR30270. 1 hit.
PfamiPF00586. AIRS. 1 hit.
[Graphical view]
PIRSFiPIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR01379. thiL. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTHIL_AQUAE
AccessioniPrimary (citable) accession number: O67883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.