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P76422 (THID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. 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
Synonyms:thiJ
Ordered Locus Names:b2103, JW2090
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.

Catalytic activity

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. Ref.1

ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Ref.1

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

Monomer. Ref.1

Sequence similarities

Belongs to the ThiD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
PRO_0000192018

Sites

Binding site441Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P76422 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E555CEFE445B8F0A

FASTA26628,634
        10         20         30         40         50         60 
MKRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTRGVQ SVYRIEPDFV 

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

       130        140        150        160        170        180 
AVATLRSRLL PQVSLITPNL PEAAALLDAP HARTEQEMLE QGRSLLAMGC GAVLMKGGHL 

       190        200        210        220        230        240 
DDEQSPDWLF TREGEQRFTA PRIMTKNTHG TGCTLSAALA ALRPRHTNWA DTVQEAKSWL 

       250        260 
SSALAQADTL EVGHGIGPVH HFHAWW 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase."
Mizote T., Tsuda M., Smith D.D.S., Nakayama H., Nakazawa T.
Microbiology 145:495-501(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBUNIT.
Strain: K12.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84200 Genomic DNA. Translation: BAA76742.1.
U00096 Genomic DNA. Translation: AAC75164.1.
AP009048 Genomic DNA. Translation: BAA15971.1.
PIRF64977.
RefSeqNP_416606.1. NC_000913.3.
YP_490343.1. NC_007779.1.

3D structure databases

ProteinModelPortalP76422.
SMRP76422. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6867N.
IntActP76422. 7 interactions.
STRING511145.b2103.

Proteomic databases

PaxDbP76422.
PRIDEP76422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75164; AAC75164; b2103.
BAA15971; BAA15971; BAA15971.
GeneID12932542.
946459.
KEGGecj:Y75_p2065.
eco:b2103.
PATRIC32119539. VBIEscCol129921_2180.

Organism-specific databases

EchoBASEEB3821.
EcoGeneEG14068. thiD.

Phylogenomic databases

eggNOGCOG0351.
HOGENOMHOG000225275.
KOK00941.
OMATNHWAYS.
OrthoDBEOG6XWV53.
PhylomeDBP76422.

Enzyme and pathway databases

BioCycEcoCyc:HMP-P-KIN-MONOMER.
ECOL316407:JW2090-MONOMER.
MetaCyc:HMP-P-KIN-MONOMER.
UniPathwayUPA00060; UER00137.
UPA00060; UER00138.

Gene expression databases

GenevestigatorP76422.

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

PROP76422.

Entry information

Entry nameTHID_ECOLI
AccessionPrimary (citable) accession number: P76422
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 102 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene