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Q9PBC5

- HISX_XYLFA

UniProt

Q9PBC5 - HISX_XYLFA

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Xylella fastidiosa (strain 9a5c)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 sitei189 – 1891NADUniRule annotation
    Binding sitei212 – 2121NADUniRule annotation
    Binding sitei237 – 2371SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Active sitei326 – 3261Proton acceptorUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Metal bindingi360 – 3601ZincUniRule annotation
    Binding sitei360 – 3601SubstrateUniRule annotation
    Binding sitei414 – 4141SubstrateUniRule annotation
    Metal bindingi419 – 4191ZincUniRule annotation
    Binding sitei419 – 4191SubstrateUniRule 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

    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:XF_2219
    OrganismiXylella fastidiosa (strain 9a5c)
    Taxonomic identifieri160492 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
    ProteomesiUP000000812: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Histidinol dehydrogenasePRO_0000135885Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi160492.XF2219.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PBC5.
    SMRiQ9PBC5. Positions 2-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    KOiK00013.
    OMAiYAAKLCG.
    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.

    Q9PBC5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIIDWNQLD TAAQAQTLTR PAQTIATQTR EAVAALIEQV RRGGDTALRD    50
    ITARLDGVDL ATFEVTAAEL AAAATAVAPE LQHAMQTAAA RIEAFHRAGM 100
    TNGYRVETAP GVVCERLVRP IARVGLYVPA GSAPLFSTAL MLGVPARLAG 150
    CREVVLCTPP SKDGRANPAV LLAARLTGVT RVFTLGGAQA IAAMAYGTAS 200
    VPTCDKVFGP GNSFVTEAKQ QLAQAGVVAI DMPAGPSEVL VIADAAANPA 250
    FIAADLLSQA EHGPDSQVLL LSDSDALMTA VQTALALQLQ QLSRAEIARQ 300
    ALAQSRLIKV ATLETAFDIS NRYAPEHLIL ALRQPRAWLH RVAAAGSVFL 350
    GDYTPEALGD YCSGTNHVLP TGGAARAYSG VSVSSFQNMI SVQAASRSGI 400
    AEIGDCALTL ARAEGLDAHA NAVALRMGTV P 431
    Length:431
    Mass (Da):44,761
    Last modified:October 1, 2000 - v1
    Checksum:iE2F6E714417279CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003849 Genomic DNA. Translation: AAF85018.1.
    PIRiF82585.
    RefSeqiNP_299498.1. NC_002488.3.

    Genome annotation databases

    EnsemblBacteriaiAAF85018; AAF85018; XF_2219.
    GeneIDi1127772.
    KEGGixfa:XF2219.
    PATRICi24134682. VBIXylFas578_2361.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003849 Genomic DNA. Translation: AAF85018.1 .
    PIRi F82585.
    RefSeqi NP_299498.1. NC_002488.3.

    3D structure databases

    ProteinModelPortali Q9PBC5.
    SMRi Q9PBC5. Positions 2-429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160492.XF2219.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF85018 ; AAF85018 ; XF_2219 .
    GeneIDi 1127772.
    KEGGi xfa:XF2219.
    PATRICi 24134682. VBIXylFas578_2361.

    Phylogenomic databases

    eggNOGi COG0141.
    KOi K00013.
    OMAi YAAKLCG.
    OrthoDBi EOG6CVVCR.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    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 the plant pathogen Xylella fastidiosa."
      Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A.
      , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
      Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 9a5c.

    Entry informationi

    Entry nameiHISX_XYLFA
    AccessioniPrimary (citable) accession number: Q9PBC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 87 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