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Q5F7D8

- HISX_NEIG1

UniProt

Q5F7D8 - HISX_NEIG1

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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 sitei130 – 1301NADUniRule annotation
    Binding sitei191 – 1911NADUniRule annotation
    Binding sitei214 – 2141NADUniRule annotation
    Binding sitei237 – 2371SubstrateUniRule annotation
    Metal bindingi259 – 2591ZincUniRule annotation
    Binding sitei259 – 2591SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Active sitei327 – 3271Proton acceptorUniRule annotation
    Active sitei328 – 3281Proton acceptorUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Metal bindingi361 – 3611ZincUniRule annotation
    Binding sitei361 – 3611SubstrateUniRule annotation
    Binding sitei415 – 4151SubstrateUniRule annotation
    Metal bindingi420 – 4201ZincUniRule annotation
    Binding sitei420 – 4201SubstrateUniRule 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

    BioCyciNGON242231:GI2G-1152-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:NGO1240
    OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
    Taxonomic identifieri242231 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000535: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Histidinol dehydrogenasePRO_0000135800Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi242231.NGO1240.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5F7D8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiCAIANRI.
    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.

    Q5F7D8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE    50
    YTNKFDQTNA KSIDDLILTQ ADLNAAFERI PNDVQTALQT AARRVESYHQ 100
    RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH 150
    VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAIAALAYGT 200
    ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD 250
    WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA 300
    SLGNRGAMIL VKDLNEACEI SNYISPEHLE LSVENPQEWA KKIRHAGAIF 350
    MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG 400
    AQKLGETASV LAHGESLTAH ARAAEFRMK 429
    Length:429
    Mass (Da):46,381
    Last modified:March 15, 2005 - v1
    Checksum:i1308394D43951E17
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW89899.1.
    RefSeqiYP_208311.1. NC_002946.2.

    Genome annotation databases

    EnsemblBacteriaiAAW89899; AAW89899; NGO1240.
    GeneIDi3282462.
    KEGGingo:NGO1240.
    PATRICi20335799. VBINeiGon24812_1459.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW89899.1 .
    RefSeqi YP_208311.1. NC_002946.2.

    3D structure databases

    ProteinModelPortali Q5F7D8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 242231.NGO1240.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW89899 ; AAW89899 ; NGO1240 .
    GeneIDi 3282462.
    KEGGi ngo:NGO1240.
    PATRICi 20335799. VBINeiGon24812_1459.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci NGON242231:GI2G-1152-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 complete genome sequence of Neisseria gonorrhoeae."
      Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
      , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700825 / FA 1090.

    Entry informationi

    Entry nameiHISX_NEIG1
    AccessioniPrimary (citable) accession number: Q5F7D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 70 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