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Protein

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase

Gene

thiD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.1 Publication
ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydroxymethylpyrimidine kinase activity Source: UniProtKB-EC
  3. phosphomethylpyrimidine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. thiamine biosynthetic process Source: UniProtKB-KW
  2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU11710-MONOMER.
MetaCyc:BSU11710-MONOMER.
UniPathwayiUPA00060; UER00137.
UPA00060; UER00138.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:thiD
Synonyms:yjbV
Ordered Locus Names:BSU11710
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU11710. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Hydroxymethylpyrimidine/phosphomethylpyrimidine kinasePRO_0000391753Add
BLAST

Proteomic databases

PaxDbiO31620.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU11710.

Structurei

3D structure databases

ProteinModelPortaliO31620.
SMRiO31620. Positions 3-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ThiD family.Curated

Phylogenomic databases

eggNOGiCOG0351.
HOGENOMiHOG000225273.
InParanoidiO31620.
KOiK00941.
OMAiHFHALWN.
OrthoDBiEOG6XWV53.
PhylomeDBiO31620.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.

Sequencei

Sequence statusi: Complete.

O31620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIYKALTIA GSDSGGGAGI QADIKTFQEL DVFGMSAITA VTAQNTLGVH
60 70 80 90 100
GVHPLTVETL RQQIDAVAED LRPDAVKTGM LWNADMIEEV ARKIDEYGFN
110 120 130 140 150
RVIVDPVMIA KGGASLLRDE SVATLKELLI PRSYAITPNV PEAETLTGMT
160 170 180 190 200
ISSLDDRKKA AEQLVKMGAQ HVIIKGGHQP EDNHITDLLF DGSMFMQITH
210 220 230 240 250
PYINTKHTHG TGCTFAAALT AQTAKGDSIH QAFEVAANFV REAVENTLGI
260 270
GSGHGPTNHF AFKRNSLNTS R
Length:271
Mass (Da):29,124
Last modified:January 1, 1998 - v1
Checksum:i1554AD7F253F983D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13028.1.
PIRiF69845.
RefSeqiNP_389053.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13028; CAB13028; BSU11710.
GeneIDi936415.
KEGGibsu:BSU11710.
PATRICi18974059. VBIBacSub10457_1223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13028.1.
PIRiF69845.
RefSeqiNP_389053.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO31620.
SMRiO31620. Positions 3-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU11710.

Proteomic databases

PaxDbiO31620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13028; CAB13028; BSU11710.
GeneIDi936415.
KEGGibsu:BSU11710.
PATRICi18974059. VBIBacSub10457_1223.

Organism-specific databases

GenoListiBSU11710. [Micado]

Phylogenomic databases

eggNOGiCOG0351.
HOGENOMiHOG000225273.
InParanoidiO31620.
KOiK00941.
OMAiHFHALWN.
OrthoDBiEOG6XWV53.
PhylomeDBiO31620.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00137.
UPA00060; UER00138.
BioCyciBSUB:BSU11710-MONOMER.
MetaCyc:BSU11710-MONOMER.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTHID_BACSU
AccessioniPrimary (citable) accession number: O31620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.