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Q81T62

- HISX_BACAN

UniProt

Q81T62 - HISX_BACAN

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei127 – 1271NADUniRule annotation
    Binding sitei188 – 1881NADUniRule annotation
    Binding sitei211 – 2111NADUniRule annotation
    Binding sitei234 – 2341SubstrateUniRule annotation
    Metal bindingi256 – 2561ZincUniRule annotation
    Binding sitei256 – 2561SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Active sitei324 – 3241Proton acceptorUniRule annotation
    Active sitei325 – 3251Proton acceptorUniRule annotation
    Binding sitei325 – 3251SubstrateUniRule annotation
    Metal bindingi358 – 3581ZincUniRule annotation
    Binding sitei358 – 3581SubstrateUniRule annotation
    Binding sitei412 – 4121SubstrateUniRule annotation
    Metal bindingi417 – 4171ZincUniRule annotation
    Binding sitei417 – 4171SubstrateUniRule annotation

    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

    BioCyciANTHRA:HISD-MONOMER.
    BANT260799:GJAJ-1391-MONOMER.
    BANT261594:GJ7F-1453-MONOMER.
    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
    Short name:
    HDHUniRule annotation
    Gene namesi
    Name:hisDUniRule annotation
    Ordered Locus Names:BA_1426, GBAA_1426, BAS1317
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Histidinol dehydrogenasePRO_0000135720Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi198094.BA_1426.

    Structurei

    3D structure databases

    ProteinModelPortaliQ81T62.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiICGPGNK.
    OrthoDBiEOG6CVVCR.

    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.

    Q81T62-1 [UniParc]FASTAAdd to Basket

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    MEIVCEDFQK ALTKIKLLRE NANIIEETVQ RSVREIVQNV RESRDEALSF    50
    YTKKFDGVEI KDVRVSEEEI KQASMFVESS FLEALQEAKK NIISYHEKQK 100
    RQSMFDCTSK GIIRGQIIRP LENIGVYVPG GTASYPSSVL MNVLPAKLAG 150
    VKKIVMVTPP RAGGIDPHIL VAASLAGVDE IYMIGGAQAI AALAYGTESI 200
    PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA DETGNAKYIA 250
    ADLLSQAEHD ERATAICITT NIELAKEVEK EIERQLETLP RSEIARESIN 300
    RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP 350
    YAPEPLGDYL AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEGALRD 400
    VKHHIVELAN KEGLHAHARA IQIRFGEEE 429
    Length:429
    Mass (Da):47,183
    Last modified:June 1, 2003 - v1
    Checksum:iEBE075B15321CD2C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25369.1.
    AE017334 Genomic DNA. Translation: AAT30522.1.
    AE017225 Genomic DNA. Translation: AAT53637.1.
    RefSeqiNP_843883.1. NC_003997.3.
    YP_018047.1. NC_007530.2.
    YP_027586.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP25369; AAP25369; BA_1426.
    AAT30522; AAT30522; GBAA_1426.
    AAT53637; AAT53637; BAS1317.
    GeneIDi1085728.
    2814920.
    2850851.
    KEGGiban:BA_1426.
    bar:GBAA_1426.
    bat:BAS1317.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25369.1 .
    AE017334 Genomic DNA. Translation: AAT30522.1 .
    AE017225 Genomic DNA. Translation: AAT53637.1 .
    RefSeqi NP_843883.1. NC_003997.3.
    YP_018047.1. NC_007530.2.
    YP_027586.1. NC_005945.1.

    3D structure databases

    ProteinModelPortali Q81T62.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198094.BA_1426.

    Protocols and materials databases

    DNASUi 1085728.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP25369 ; AAP25369 ; BA_1426 .
    AAT30522 ; AAT30522 ; GBAA_1426 .
    AAT53637 ; AAT53637 ; BAS1317 .
    GeneIDi 1085728.
    2814920.
    2850851.
    KEGGi ban:BA_1426.
    bar:GBAA_1426.
    bat:BAS1317.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi ICGPGNK.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci ANTHRA:HISD-MONOMER.
    BANT260799:GJAJ-1391-MONOMER.
    BANT261594:GJ7F-1453-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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.

    Entry informationi

    Entry nameiHISX_BACAN
    AccessioniPrimary (citable) accession number: Q81T62
    Secondary accession number(s): Q6I1E5, Q6KV91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 88 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3