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E8YFB9 (E8YFB9_9BURK) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiamine-monophosphate kinase HAMAP-Rule MF_02128
Short name=TMP kinase HAMAP-Rule MF_02128
Short name=Thiamine-phosphate kinase HAMAP-Rule MF_02128
EC=2.7.4.16 HAMAP-Rule MF_02128
Gene names
Name:thiL HAMAP-Rule MF_02128
ORF Names:BC1001_3041 EMBL ADX56455.1
OrganismBurkholderia sp. CCGE1001 EMBL ADX56455.1
Taxonomic identifier640510 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1 By similarity. HAMAP-Rule MF_02128

Catalytic activity

ATP + thiamine phosphate = ADP + thiamine diphosphate. HAMAP-Rule MF_02128

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1. HAMAP-Rule MF_02128

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 By similarity. HAMAP-Rule MF_02128

Sequence similarities

Belongs to the thiamine-monophosphate kinase family. HAMAP-Rule MF_02128

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding124 – 1252ATP By similarity HAMAP-Rule MF_02128

Sites

Metal binding331Magnesium 3 By similarity HAMAP-Rule MF_02128
Metal binding331Magnesium 4; via carbonyl oxygen By similarity HAMAP-Rule MF_02128
Metal binding481Magnesium 4 By similarity HAMAP-Rule MF_02128
Metal binding491Magnesium 1; via carbonyl oxygen By similarity HAMAP-Rule MF_02128
Metal binding501Magnesium 1 By similarity HAMAP-Rule MF_02128
Metal binding501Magnesium 2 By similarity HAMAP-Rule MF_02128
Metal binding781Magnesium 2 By similarity HAMAP-Rule MF_02128
Metal binding781Magnesium 3 By similarity HAMAP-Rule MF_02128
Metal binding781Magnesium 4 By similarity HAMAP-Rule MF_02128
Metal binding1251Magnesium 1 By similarity HAMAP-Rule MF_02128
Metal binding2141Magnesium 3 By similarity HAMAP-Rule MF_02128
Metal binding2171Magnesium 5 By similarity HAMAP-Rule MF_02128
Binding site571Substrate By similarity HAMAP-Rule MF_02128
Binding site1491ATP By similarity HAMAP-Rule MF_02128
Binding site2161ATP By similarity HAMAP-Rule MF_02128
Binding site2641Substrate By similarity HAMAP-Rule MF_02128
Binding site3261Substrate By similarity HAMAP-Rule MF_02128

Sequences

Sequence LengthMass (Da)Tools
E8YFB9 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: CCD7E4DB349CB49E

FASTA33234,698
        10         20         30         40         50         60 
MLSEFSLIER FFARRAAGQP SPAANGSLGI GDDCALIAPR AGQMLAISTD MLVEGRHFFP 

        70         80         90        100        110        120 
DVDPEALGHK ALAVNLSDLA AMGAQPQAFT LAFALPKADE AWLAAFSEGL FALAERHGCA 

       130        140        150        160        170        180 
LIGGDTTGGP LNLCITVFGS VPPHTALRRD AAQPGDDIWV SGTLGDARAG LGIQRGEWSA 

       190        200        210        220        230        240 
DSADAAFFRR ALERPEPRIA LGLALRGVAH AALDVSDGLA GDLKHILDRS NVRATVDADA 

       250        260        270        280        290        300 
VPRSAALRRL PLDTQRRCTL AGGDDYELCF TAPPAARGAV DNAGRTAGVP VTRIGTISAL 

       310        320        330 
QTAADRPAID WRNAAGAPLT LTLQGFDHFH AD

« Hide

References

[1]"Complete sequence of chromosome1 of Burkholderia sp. CCGE1001."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Martinez-Romero E. expand/collapse author list , Rogel M.A., Auchtung J., Tiedje J., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CCGE1001 EMBL ADX56455.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002519 Genomic DNA. Translation: ADX56455.1.
RefSeqYP_004229515.1. NC_015136.1.

3D structure databases

ProteinModelPortalE8YFB9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX56455; ADX56455; BC1001_3041.
GeneID10224614.
KEGGbug:BC1001_3041.
PATRIC46898953. VBIBurSp1058_3183.

Phylogenomic databases

KOK00946.

Enzyme and pathway databases

BioCycBSP640510:GI28-3092-MONOMER.
UniPathwayUPA00060; UER00142.

Family and domain databases

Gene3D3.90.650.10. 1 hit.
HAMAPMF_02128. TMP_kinase.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR016188. PurM_N-like.
IPR006283. ThiL.
[Graphical view]
PANTHERPTHR30270. PTHR30270. 1 hit.
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFPIRSF005303. Thiam_monoph_kin. 1 hit.
SUPFAMSSF56042. AIR_synth_C. 1 hit.
SSF55326. PurM_N-like. 1 hit.
TIGRFAMsTIGR01379. thiL. 1 hit.
ProtoNetSearch...

Entry information

Entry nameE8YFB9_9BURK
AccessionPrimary (citable) accession number: E8YFB9
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: May 29, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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