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O31620 (THID_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 74. 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:yjbV
Ordered Locus Names:BSU11710
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length271 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. Ref.2

Catalytic activity

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

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

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.

Sequence similarities

Belongs to the ThiD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
PRO_0000391753

Sites

Binding site441Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O31620 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1554AD7F253F983D

FASTA27129,124
        10         20         30         40         50         60 
MSIYKALTIA GSDSGGGAGI QADIKTFQEL DVFGMSAITA VTAQNTLGVH GVHPLTVETL 

        70         80         90        100        110        120 
RQQIDAVAED LRPDAVKTGM LWNADMIEEV ARKIDEYGFN RVIVDPVMIA KGGASLLRDE 

       130        140        150        160        170        180 
SVATLKELLI PRSYAITPNV PEAETLTGMT ISSLDDRKKA AEQLVKMGAQ HVIIKGGHQP 

       190        200        210        220        230        240 
EDNHITDLLF DGSMFMQITH PYINTKHTHG TGCTFAAALT AQTAKGDSIH QAFEVAANFV 

       250        260        270 
REAVENTLGI GSGHGPTNHF AFKRNSLNTS R 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and pyridoxal kinase."
Park J.-H., Burns K., Kinsland C., Begley T.P.
J. Bacteriol. 186:1571-1573(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS HMP AND HMP-P KINASE, CATALYTIC ACTIVITY.
Strain: 168 / CU1065.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB13028.1.
PIRF69845.
RefSeqNP_389053.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31620.
SMRO31620. Positions 3-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU11710.

Proteomic databases

PaxDbO31620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13028; CAB13028; BSU11710.
GeneID936415.
KEGGbsu:BSU11710.
PATRIC18974059. VBIBacSub10457_1223.

Organism-specific databases

GenoListBSU11710. [Micado]

Phylogenomic databases

eggNOGCOG0351.
HOGENOMHOG000225273.
KOK00941.
OMAHFHALWN.
OrthoDBEOG6XWV53.
ProtClustDBPRK06427.

Enzyme and pathway databases

BioCycBSUB:BSU11710-MONOMER.
MetaCyc:BSU11710-MONOMER.
UniPathwayUPA00060; UER00137.
UPA00060; UER00138.

Family and domain databases

InterProIPR013749. HMP-P_kinase-1.
IPR004399. HMP-P_kinase-2.
[Graphical view]
PfamPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
TIGRFAMsTIGR00097. HMP-P_kinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHID_BACSU
AccessionPrimary (citable) accession number: O31620
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 74 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList