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Q6FEC8

- HISX_ACIAD

UniProt

Q6FEC8 - HISX_ACIAD

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      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 sitei131 – 1311NADUniRule annotation
    Binding sitei192 – 1921NADUniRule annotation
    Binding sitei215 – 2151NADUniRule annotation
    Binding sitei238 – 2381SubstrateUniRule annotation
    Metal bindingi260 – 2601ZincUniRule annotation
    Binding sitei260 – 2601SubstrateUniRule annotation
    Metal bindingi263 – 2631ZincUniRule annotation
    Binding sitei263 – 2631SubstrateUniRule annotation
    Active sitei328 – 3281Proton acceptorUniRule annotation
    Active sitei329 – 3291Proton acceptorUniRule annotation
    Binding sitei329 – 3291SubstrateUniRule annotation
    Metal bindingi362 – 3621ZincUniRule annotation
    Binding sitei362 – 3621SubstrateUniRule annotation
    Binding sitei416 – 4161SubstrateUniRule annotation
    Metal bindingi421 – 4211ZincUniRule annotation
    Binding sitei421 – 4211SubstrateUniRule 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

    BioCyciASP62977:GJVV-626-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:ACIAD0663
    OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    Taxonomic identifieri62977 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    ProteomesiUP000000430: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Histidinol dehydrogenasePRO_0000135713Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi62977.ACIAD0663.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FEC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    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.

    Q6FEC8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRRLSTQDQ SFKQVFADLL AFETVNDPEL LKTVDQIIAD VRQYGDEHVL    50
    KLTQQFDRHP AHQFSDLELT QEQLKTAFEA LTAEIREALE LAAERIRSFH 100
    QAQKQEGWSY VDALGNTLGQ KVTPLDRVGI YVPGGLASYP SSVLMNAIPA 150
    HVAGVPEIIM VVPAPNGELN SLVLAAAYLA GVSRIFTIGG AQAVAALAYG 200
    TQTIPAVDKI TGPGNRFVAA AKRAVFGQVG IDMIAGPSEI LVYAEGQNNA 250
    KWLAMDLLSQ AEHDTVAQAI FITPDEALLD EVAQAIEEHL AALPKADIAR 300
    TSIANRGALV LVKDRDEAIE LINQVAPEHL ELCLDESEAM SQKIRHAGAI 350
    FMGRYTPEAI GDYCAGPNHV LPTSGTARFS SPLGVYDFQK RSSLIMCSQE 400
    GVKSLAKAAD VLAQQENLDA HARSARYRYQ 430
    Length:430
    Mass (Da):46,671
    Last modified:July 19, 2004 - v1
    Checksum:i75B7CFF03AB94510
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67580.1.
    RefSeqiWP_011182111.1. NC_005966.1.
    YP_045402.1. NC_005966.1.

    Genome annotation databases

    EnsemblBacteriaiCAG67580; CAG67580; ACIAD0663.
    GeneIDi2878926.
    KEGGiaci:ACIAD0663.
    PATRICi20739230. VBIAciSp98416_0585.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67580.1 .
    RefSeqi WP_011182111.1. NC_005966.1.
    YP_045402.1. NC_005966.1.

    3D structure databases

    ProteinModelPortali Q6FEC8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 62977.ACIAD0663.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG67580 ; CAG67580 ; ACIAD0663 .
    GeneIDi 2878926.
    KEGGi aci:ACIAD0663.
    PATRICi 20739230. VBIAciSp98416_0585.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci ASP62977:GJVV-626-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
      Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
      Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33305 / BD413 / ADP1.

    Entry informationi

    Entry nameiHISX_ACIAD
    AccessioniPrimary (citable) accession number: Q6FEC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 77 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