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Protein

Thiamine-monophosphate kinase

Gene

thiL

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

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 bindingi30Magnesium 3UniRule annotation1
Metal bindingi30Magnesium 4; via carbonyl oxygenUniRule annotation1
Metal bindingi45Magnesium 4UniRule annotation1
Metal bindingi46Magnesium 1; via carbonyl oxygenUniRule annotation1
Metal bindingi47Magnesium 1UniRule annotation1
Metal bindingi47Magnesium 2UniRule annotation1
Binding sitei54SubstrateUniRule annotation1
Metal bindingi75Magnesium 2UniRule annotation1
Metal bindingi75Magnesium 3UniRule annotation1
Metal bindingi75Magnesium 4UniRule annotation1
Metal bindingi122Magnesium 1UniRule annotation1
Binding sitei146ATPUniRule annotation1
Metal bindingi211Magnesium 3UniRule annotation1
Binding sitei213ATPUniRule annotation1
Metal bindingi214Magnesium 5UniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Binding sitei314SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi121 – 122ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Biological processi

Thiamine biosynthesisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

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:thiLUniRule annotationImported
Ordered Locus Names:PA4051Imported
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)Imported
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4051.

PTM / Processingi

Proteomic databases

PaxDbiQ9HWX7.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4051.

Structurei

3D structure databases

ProteinModelPortaliQ9HWX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 138AIRSInterPro annotationAdd BLAST110
Domaini150 – 297AIRS_CInterPro annotationAdd BLAST148

Sequence similaritiesi

Belongs to the thiamine-monophosphate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CG2. Bacteria.
COG0611. LUCA.
HOGENOMiHOG000228429.
InParanoidiQ9HWX7.
KOiK00946.
OMAiDIYAMNA.
PhylomeDBiQ9HWX7.

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.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR01379. thiL. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HWX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEFELIRRF FAAAACAAPA ADVALGIGDD CALLAPPAGE QLAVSTDTLV
60 70 80 90 100
EGVHFPAGCD PFLLAQRALA VSASDLAAMG AAPLAFTLAL TLPQADAEWL
110 120 130 140 150
QGFARGLDAM ARQCGLALVG GDTTRGPLSM TLTVFGRVPA GQALTRAGAR
160 170 180 190 200
PGDLLCVGGP LGEAGAALEL VLERRSAPAE VAEPLLARYW TPAPQFGLGL
210 220 230 240 250
ALRGKASAAL DISDGLLADC GHIARASGVA LLVECQRLQA SAALSGLLAG
260 270 280 290 300
EEALRQQLAA GDDYVLVFTL PPEYLGEIRA AWPAMAVIGR VEAGQGVHLL
310 320
DADGKELIPA AAGYQHFGTQ RD
Length:322
Mass (Da):32,912
Last modified:March 1, 2001 - v1
Checksum:i259FD10122DDCF4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07438.1.
PIRiF83140.
RefSeqiNP_252740.1. NC_002516.2.
WP_003113052.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG07438; AAG07438; PA4051.
GeneIDi878642.
KEGGipae:PA4051.
PATRICi19842771. VBIPseAer58763_4242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07438.1.
PIRiF83140.
RefSeqiNP_252740.1. NC_002516.2.
WP_003113052.1. NC_002516.2.

3D structure databases

ProteinModelPortaliQ9HWX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4051.

Proteomic databases

PaxDbiQ9HWX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07438; AAG07438; PA4051.
GeneIDi878642.
KEGGipae:PA4051.
PATRICi19842771. VBIPseAer58763_4242.

Organism-specific databases

PseudoCAPiPA4051.

Phylogenomic databases

eggNOGiENOG4105CG2. Bacteria.
COG0611. LUCA.
HOGENOMiHOG000228429.
InParanoidiQ9HWX7.
KOiK00946.
OMAiDIYAMNA.
PhylomeDBiQ9HWX7.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00142.

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.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAMiSSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR01379. thiL. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ9HWX7_PSEAE
AccessioniPrimary (citable) accession number: Q9HWX7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: October 5, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.