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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Magnesium 31 Publication
Metal bindingi27 – 271Magnesium 4; via carbonyl oxygen1 Publication
Metal bindingi41 – 411Magnesium 41 Publication
Metal bindingi42 – 421Magnesium 1; via carbonyl oxygen1 Publication
Metal bindingi43 – 431Magnesium 11 Publication
Metal bindingi43 – 431Magnesium 21 Publication
Binding sitei50 – 501Substrate1 Publication
Metal bindingi71 – 711Magnesium 21 Publication
Metal bindingi71 – 711Magnesium 31 Publication
Metal bindingi71 – 711Magnesium 41 Publication
Binding sitei101 – 1011ATP1 Publication
Metal bindingi119 – 1191Magnesium 11 Publication
Binding sitei142 – 1421ATP1 Publication
Metal bindingi207 – 2071Magnesium 31 Publication
Binding sitei209 – 2091ATP1 Publication
Metal bindingi210 – 2101Magnesium 51 Publication
Binding sitei260 – 2601Substrate1 Publication
Binding sitei303 – 3031Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi118 – 1192ATP1 Publication

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

BioCyciAAEO224324:GJBH-1515-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Thiamine-monophosphate kinasePRO_0000415517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 – 34Interchain1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224324.aq_2119.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi8 – 1912Combined sources
Beta strandi26 – 338Combined sources
Beta strandi36 – 4611Combined sources
Turni47 – 493Combined sources
Helixi57 – 7418Combined sources
Beta strandi78 – 8811Combined sources
Helixi94 – 11118Combined sources
Beta strandi114 – 1229Combined sources
Beta strandi127 – 13812Combined sources
Beta strandi150 – 1556Combined sources
Helixi159 – 16810Combined sources
Helixi176 – 18611Combined sources
Helixi192 – 1943Combined sources
Helixi195 – 2017Combined sources
Beta strandi203 – 2108Combined sources
Helixi212 – 22312Combined sources
Beta strandi226 – 2294Combined sources
Helixi231 – 2333Combined sources
Helixi238 – 2469Combined sources
Helixi251 – 2577Combined sources
Beta strandi263 – 2686Combined sources
Helixi270 – 2723Combined sources
Turni275 – 2784Combined sources
Beta strandi279 – 29315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-306.
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.
OrthoDBiEOG6RRKQ4.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_02128. TMP_kinase.
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
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. Positions 1-306.
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.
OrthoDBiEOG6RRKQ4.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00142.
BioCyciAAEO224324:GJBH-1515-MONOMER.
BRENDAi2.7.4.16. 396.

Miscellaneous databases

EvolutionaryTraceiO67883.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_02128. TMP_kinase.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Structural studies of thiamin monophosphate kinase in complex with substrates and products."
    McCulloch K.M., Kinsland C., Begley T.P., Ealick S.E.
    Biochemistry 47:3810-3821(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH ATP; ADP; TMP; TPP AND MAGNESIUM, FUNCTION, DISULFIDE BOND, SUBUNIT, REACTION MECHANISM.
  3. "Crystal structure of thiamine monophosphate kinase (ThiL) from Aquifex Aeolicus."
    New York structural genomics research consortium (NYSGRC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).

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: May 11, 2016
This is version 97 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.