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P55882 (THID_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
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 names
Name:thiD
Ordered Locus Names:STM2146
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the ThiD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
PRO_0000192026

Sites

Binding site441Substrate

Experimental info

Sequence conflict441Q → E in AAB66492. Ref.1

Secondary structure

............................................ 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55882 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: F8B94332E1616368

FASTA26628,544
        10         20         30         40         50         60 
MQRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTCGVQ SVYRIEPDFV 

        70         80         90        100        110        120 
AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRHHVR NVVLDTVMLA KSGDPLLSPS 

       130        140        150        160        170        180 
AIETLRVRLL PQVSLITPNL PEAAALLDAP HARTEQEMLA QGRALLAMGC EAVLMKGGHL 

       190        200        210        220        230        240 
EDAQSPDWLF TREGEQRFSA PRVNTKNTHG TGCTLSAALA ALRPRHRSWG ETVNEAKAWL 

       250        260 
SAALAQADTL EVGKGIGPVH HFHAWW 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis."
Petersen L.A., Downs D.M.
J. Bacteriol. 179:4894-4900(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3 A resolution."
Cheng G., Bennett E.M., Begley T.P., Ealick S.E.
Structure 10:225-235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87940 Genomic DNA. Translation: AAB66492.1.
AE006468 Genomic DNA. Translation: AAL21049.1.
RefSeqNP_461090.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXHX-ray2.30A/B1-266[»]
1JXIX-ray2.64A/B1-266[»]
1LLJmodel-A1-266[»]
ProteinModelPortalP55882.
SMRP55882. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2146.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21049; AAL21049; STM2146.
GeneID1253667.
KEGGstm:STM2146.
PATRIC32382881. VBISalEnt20916_2271.

Phylogenomic databases

eggNOGCOG0351.
HOGENOMHOG000225275.
KOK00941.
OMATNHWAYS.
OrthoDBEOG6XWV53.
PhylomeDBP55882.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-6200-MONOMER.
SENT99287:GCTI-2159-MONOMER.
UniPathwayUPA00060; UER00137.
UPA00060; UER00138.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
InterProIPR013749. HMP-P_kinase-1.
IPR004399. HMP-P_kinase-2.
IPR029056. Ribokinase-like.
[Graphical view]
PfamPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMSSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00097. HMP-P_kinase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP55882.

Entry information

Entry nameTHID_SALTY
AccessionPrimary (citable) accession number: P55882
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways