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Q3A133

- HISX_PELCD

UniProt

Q3A133 - HISX_PELCD

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (22 Nov 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

    BioCyciPCAR338963:GKDU-2953-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:Pcar_2688
    OrganismiPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
    Taxonomic identifieri338963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
    ProteomesiUP000002534: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Histidinol dehydrogenasePRO_0000135811Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi338963.Pcar_2688.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3A133.
    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.

    Q3A133-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRLLSFDDS DFGAALGAIV ARGETPPEGV EETVAEILEA VRLQGDRALL    50
    EYTTRFDGLD LTAAQLQVTA EEIEAALAAV DSESMAALQL AADRIAAFHR 100
    RQKTETWLTT DEQDVMLGQM VQPLERVGIY VPGGKASYPS SVLMNAIPAK 150
    VAGVAEVVMV VPMPHGEVNP HVLAAAHLAG VDRIFKIGGA QAVAALAYGT 200
    ESVPRVDKIT GPGNIYVATA KKMVFGQVDI DMIAGPSEIL VINDGSGTPE 250
    HIAVDLLSQA EHDELAAAIL VTTDADFGRR VQQAVEEQLA TLKRAAIARC 300
    SIDAFGAILV ARDLEQAVAL SNSIAPEHLE LAVDDPFSLL PRIRHAGAIF 350
    MGHHCPEAAG DYLAGPNHTL PTGGTARFFS PLGVDDFVKK SSIISFSREG 400
    LDRLGRSIVH LAELEGLEAH GRSVSIRLKD S 431
    Length:431
    Mass (Da):45,770
    Last modified:November 22, 2005 - v1
    Checksum:i9095B283C1766595
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000142 Genomic DNA. Translation: ABA89924.1.
    RefSeqiWP_011342467.1. NC_007498.2.
    YP_006718465.1. NC_007498.2.

    Genome annotation databases

    EnsemblBacteriaiABA89924; ABA89924; Pcar_2688.
    GeneIDi3725393.
    KEGGipca:Pcar_2688.
    PATRICi22891754. VBIPelCar86875_2915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000142 Genomic DNA. Translation: ABA89924.1 .
    RefSeqi WP_011342467.1. NC_007498.2.
    YP_006718465.1. NC_007498.2.

    3D structure databases

    ProteinModelPortali Q3A133.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338963.Pcar_2688.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA89924 ; ABA89924 ; Pcar_2688 .
    GeneIDi 3725393.
    KEGGi pca:Pcar_2688.
    PATRICi 22891754. VBIPelCar86875_2915.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PCAR338963:GKDU-2953-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. "Complete sequence of Pelobacter carbinolicus DSM 2380."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2380 / Gra Bd 1.

    Entry informationi

    Entry nameiHISX_PELCD
    AccessioniPrimary (citable) accession number: Q3A133
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 67 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