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Q4FQF8

- HISX_PSYA2

UniProt

Q4FQF8 - HISX_PSYA2

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (30 Aug 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 bindingi261 – 2611ZincUniRule annotation
    Binding sitei261 – 2611SubstrateUniRule annotation
    Metal bindingi264 – 2641ZincUniRule annotation
    Binding sitei264 – 2641SubstrateUniRule annotation
    Active sitei329 – 3291Proton acceptorUniRule annotation
    Active sitei330 – 3301Proton acceptorUniRule annotation
    Binding sitei330 – 3301SubstrateUniRule annotation
    Metal bindingi363 – 3631ZincUniRule annotation
    Binding sitei363 – 3631SubstrateUniRule annotation
    Binding sitei417 – 4171SubstrateUniRule annotation
    Metal bindingi422 – 4221ZincUniRule annotation
    Binding sitei422 – 4221SubstrateUniRule 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

    BioCyciPARC259536:GI3A-1947-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:Psyc_1902
    OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
    Taxonomic identifieri259536 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000000546: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Histidinol dehydrogenasePRO_0000135825Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi259536.Psyc_1902.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4FQF8.
    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.

    Q4FQF8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRQLSTQDAD FDSQLTELLA FETVNDATLL TTVDDIIARV RHGGDSVVLE    50
    LTQQFDQHPA TTTQALELSK EALAEAFANL DDVVKSALIT AATRVKTFHE 100
    RQVQETWQYE DELGNRLGQK VTALDRVGIY VPGGLASYPS SVLMNAIPAK 150
    VAGVKEVIMV VPAPKGVLNP LVLAAAHLAK VDRVFTIGGA QAVAALAYGT 200
    ETIPAVDKIT GPGNKYVAAA KRAVFGQVGI DMIAGPSEVL VYAEGEAQDR 250
    ADWLAMDLLS QAEHDRIAQA IFVTTSAQQL KEVAIEIEKA LAELPKADIA 300
    RDSLKNRGVL ILVRDREEGM AVINRVAPEH LELSVDHPDA LLNSIRHAGA 350
    IFMGRHTPEA IGDYCAGPNH VLPTSGTARF SSPLGVYDFQ KKSSIIYCSE 400
    SGSKPLAQTA DILAQHEDLE AHARSARYRY Q 431
    Length:431
    Mass (Da):46,506
    Last modified:August 30, 2005 - v1
    Checksum:i0F4BC4043056A41D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ19750.1.
    RefSeqiYP_265184.1. NC_007204.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ19750; AAZ19750; Psyc_1902.
    GeneIDi3515872.
    KEGGipar:Psyc_1902.
    PATRICi23058695. VBIPsyArc98534_2252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000082 Genomic DNA. Translation: AAZ19750.1 .
    RefSeqi YP_265184.1. NC_007204.1.

    3D structure databases

    ProteinModelPortali Q4FQF8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 259536.Psyc_1902.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ19750 ; AAZ19750 ; Psyc_1902 .
    GeneIDi 3515872.
    KEGGi par:Psyc_1902.
    PATRICi 23058695. VBIPsyArc98534_2252.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PARC259536:GI3A-1947-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 Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
      Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
      Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 17307 / 273-4.

    Entry informationi

    Entry nameiHISX_PSYA2
    AccessioniPrimary (citable) accession number: Q4FQF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 71 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