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O31620

- THID_BACSU

UniProt

O31620 - THID_BACSU

Protein

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase

Gene

thiD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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.
    KOiK00941.
    OMAiVKTGMLW.
    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

    MSIYKALTIA GSDSGGGAGI QADIKTFQEL DVFGMSAITA VTAQNTLGVH    50
    GVHPLTVETL RQQIDAVAED LRPDAVKTGM LWNADMIEEV ARKIDEYGFN 100
    RVIVDPVMIA KGGASLLRDE SVATLKELLI PRSYAITPNV PEAETLTGMT 150
    ISSLDDRKKA AEQLVKMGAQ HVIIKGGHQP EDNHITDLLF DGSMFMQITH 200
    PYINTKHTHG TGCTFAAALT AQTAKGDSIH QAFEVAANFV REAVENTLGI 250
    GSGHGPTNHF AFKRNSLNTS R 271
    Length:271
    Mass (Da):29,124
    Last modified:January 1, 1998 - v1
    Checksum:i1554AD7F253F983D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13028.1 .
    PIRi F69845.
    RefSeqi NP_389053.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O31620.
    SMRi O31620. Positions 3-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU11710.

    Proteomic databases

    PaxDbi O31620.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13028 ; CAB13028 ; BSU11710 .
    GeneIDi 936415.
    KEGGi bsu:BSU11710.
    PATRICi 18974059. VBIBacSub10457_1223.

    Organism-specific databases

    GenoListi BSU11710. [Micado ]

    Phylogenomic databases

    eggNOGi COG0351.
    HOGENOMi HOG000225273.
    KOi K00941.
    OMAi VKTGMLW.
    OrthoDBi EOG6XWV53.
    PhylomeDBi O31620.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00137 .
    UPA00060 ; UER00138 .
    BioCyci BSUB:BSU11710-MONOMER.
    MetaCyc:BSU11710-MONOMER.

    Family and domain databases

    Gene3Di 3.40.1190.20. 1 hit.
    InterProi IPR004399. HMP/HMP-P_kinase.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    [Graphical view ]
    Pfami PF08543. Phos_pyr_kin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00097. HMP-P_kinase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 79 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