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Q6A8L5

- HISX_PROAC

UniProt

Q6A8L5 - HISX_PROAC

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
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 (13 Sep 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 sitei129 – 1291NADUniRule annotation
    Binding sitei193 – 1931NADUniRule annotation
    Binding sitei222 – 2221NADUniRule annotation
    Binding sitei245 – 2451SubstrateUniRule annotation
    Metal bindingi267 – 2671ZincUniRule annotation
    Binding sitei267 – 2671SubstrateUniRule annotation
    Metal bindingi270 – 2701ZincUniRule annotation
    Binding sitei270 – 2701SubstrateUniRule annotation
    Active sitei336 – 3361Proton acceptorUniRule annotation
    Active sitei337 – 3371Proton acceptorUniRule annotation
    Binding sitei337 – 3371SubstrateUniRule annotation
    Metal bindingi370 – 3701ZincUniRule annotation
    Binding sitei370 – 3701SubstrateUniRule annotation
    Binding sitei424 – 4241SubstrateUniRule annotation
    Metal bindingi429 – 4291ZincUniRule annotation
    Binding sitei429 – 4291SubstrateUniRule 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

    BioCyciPACN267747:GHO9-1165-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:PPA1152
    OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
    Taxonomic identifieri267747 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
    ProteomesiUP000000603: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Histidinol dehydrogenasePRO_0000135817Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi267747.PPA1152.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6A8L5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiQKSLHAV.
    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.

    Q6A8L5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRIVDVTSE TTDDLRCAVP RADFDVDAAM AAVIPVCSAV RDRGVEALRE    50
    YSEKFDHVVP EHLRVPVEAL ATAAANLDGT LRRAFSESIR RRRQVCQEAE 100
    VETSSQPVEV AGGARVSQRI VPVGRVGLYV PGGFAPLASS VIMNVVPAQE 150
    AGVSSIAVAS PPQAEFGGLP HPSILALCHL LGVNEVYAVG GAQAIAMFAY 200
    GVEGSDEADS CPRVDMVTGP GNIYVVAAKR CLRGTVGIDS EAGPTEIAIL 250
    ADETADPRHI AADLMSQAEH DTLAAAVLVT DSTTLAEAVQ RELAPMVSAT 300
    LHSERIRTSL TSKQSAIVMV RDIDQGLEVV NAYAAEHLEI QTADAAAVAA 350
    RVWNAGAIFV GPWAPVSLGD YSAGSTHVLP TAGAACHSSG LSVRSFMRAV 400
    HVIDYTEDAL LELADSVEAF ALAENLPGHA NAITVRRSR 439
    Length:439
    Mass (Da):46,098
    Last modified:September 13, 2004 - v1
    Checksum:iF1B7C0C567681677
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017283 Genomic DNA. Translation: AAT82901.1.
    RefSeqiYP_055859.1. NC_006085.1.

    Genome annotation databases

    EnsemblBacteriaiAAT82901; AAT82901; PPA1152.
    GeneIDi2932004.
    KEGGipac:PPA1152.
    PATRICi23037039. VBIProAcn64440_1188.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017283 Genomic DNA. Translation: AAT82901.1 .
    RefSeqi YP_055859.1. NC_006085.1.

    3D structure databases

    ProteinModelPortali Q6A8L5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267747.PPA1152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT82901 ; AAT82901 ; PPA1152 .
    GeneIDi 2932004.
    KEGGi pac:PPA1152.
    PATRICi 23037039. VBIProAcn64440_1188.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci PACN267747:GHO9-1165-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 Propionibacterium acnes, a commensal of human skin."
      Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
      Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KPA171202 / DSM 16379.

    Entry informationi

    Entry nameiHISX_PROAC
    AccessioniPrimary (citable) accession number: Q6A8L5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: September 13, 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