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O34651

- HISX_BACSU

UniProt

O34651 - HISX_BACSU

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.By similarity

    Catalytic activityi

    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231NADBy similarity
    Binding sitei185 – 1851NADBy similarity
    Binding sitei208 – 2081NADBy similarity
    Binding sitei231 – 2311SubstrateBy similarity
    Metal bindingi253 – 2531ZincBy similarity
    Binding sitei253 – 2531SubstrateBy similarity
    Metal bindingi256 – 2561ZincBy similarity
    Binding sitei256 – 2561SubstrateBy similarity
    Active sitei321 – 3211Proton acceptorBy similarity
    Active sitei322 – 3221Proton acceptorBy similarity
    Binding sitei322 – 3221SubstrateBy similarity
    Metal bindingi355 – 3551ZincBy similarity
    Binding sitei355 – 3551SubstrateBy similarity
    Binding sitei409 – 4091SubstrateBy similarity
    Metal bindingi414 – 4141ZincBy similarity
    Binding sitei414 – 4141SubstrateBy similarity

    GO - Molecular functioni

    1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
    2. NAD binding Source: InterPro
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU34910-MONOMER.
    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:hisD
    Ordered Locus Names:BSU34910
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU34910. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Histidinol dehydrogenasePRO_0000135728Add
    BLAST

    Proteomic databases

    PaxDbiO34651.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU34910.

    Structurei

    3D structure databases

    ProteinModelPortaliO34651.
    SMRiO34651. Positions 2-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiYAAKLCG.
    OrthoDBiEOG6CVVCR.
    PhylomeDBiO34651.

    Family and domain databases

    HAMAPiMF_01024. HisD.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR001692. Histidinol_DH_CS.
    IPR022695. Histidinol_DH_monofunct.
    IPR012131. Hstdl_DH.
    [Graphical view]
    PfamiPF00815. Histidinol_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
    PRINTSiPR00083. HOLDHDRGNASE.
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR00069. hisD. 1 hit.
    PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O34651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK    50
    FDCIEIDSPL VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW 100
    FYHRKDGTML GQKVTALDSA GVYVPGGTAA YPSSVLMNVI PALVAGVERI 150
    VLVTPPGKDG LLSPGVLVAA AELGIKDIYK MGGAQAIAAL AYGTETIEPV 200
    DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET AIPSEIAADL 250
    LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG 300
    CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP 350
    EPVGDYFAGP NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE 400
    SIAAFARLEG LEAHARSIEA RERRISK 427
    Length:427
    Mass (Da):46,256
    Last modified:January 1, 1998 - v1
    Checksum:iBDB0B2AE3C580E7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017113 Genomic DNA. Translation: AAC67295.1.
    AL009126 Genomic DNA. Translation: CAB15496.1.
    PIRiA69641.
    RefSeqiNP_391371.1. NC_000964.3.
    WP_003243286.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15496; CAB15496; BSU34910.
    GeneIDi936584.
    KEGGibsu:BSU34910.
    PATRICi18978988. VBIBacSub10457_3656.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017113 Genomic DNA. Translation: AAC67295.1 .
    AL009126 Genomic DNA. Translation: CAB15496.1 .
    PIRi A69641.
    RefSeqi NP_391371.1. NC_000964.3.
    WP_003243286.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali O34651.
    SMRi O34651. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU34910.

    Proteomic databases

    PaxDbi O34651.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15496 ; CAB15496 ; BSU34910 .
    GeneIDi 936584.
    KEGGi bsu:BSU34910.
    PATRICi 18978988. VBIBacSub10457_3656.

    Organism-specific databases

    GenoListi BSU34910. [Micado ]

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.
    PhylomeDBi O34651.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci BSUB:BSU34910-MONOMER.

    Family and domain databases

    HAMAPi MF_01024. HisD.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR001692. Histidinol_DH_CS.
    IPR022695. Histidinol_DH_monofunct.
    IPR012131. Hstdl_DH.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
    PRINTSi PR00083. HOLDHDRGNASE.
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR00069. hisD. 1 hit.
    PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis."
      Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.

    Entry informationi

    Entry nameiHISX_BACSU
    AccessioniPrimary (citable) accession number: O34651
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 107 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