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Q2YZB4

- HISX_STAAB

UniProt

Q2YZB4 - HISX_STAAB

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (20 Dec 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 sitei117 – 1171NADUniRule annotation
    Binding sitei178 – 1781NADUniRule annotation
    Binding sitei201 – 2011NADUniRule annotation
    Binding sitei224 – 2241SubstrateUniRule annotation
    Metal bindingi246 – 2461ZincUniRule annotation
    Binding sitei246 – 2461SubstrateUniRule annotation
    Metal bindingi249 – 2491ZincUniRule annotation
    Binding sitei249 – 2491SubstrateUniRule annotation
    Active sitei314 – 3141Proton acceptorUniRule annotation
    Active sitei315 – 3151Proton acceptorUniRule annotation
    Binding sitei315 – 3151SubstrateUniRule annotation
    Metal bindingi348 – 3481ZincUniRule annotation
    Binding sitei348 – 3481SubstrateUniRule annotation
    Binding sitei402 – 4021SubstrateUniRule annotation
    Metal bindingi407 – 4071ZincUniRule annotation
    Binding sitei407 – 4071SubstrateUniRule 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

    BioCyciSAUR273036:GJVS-2627-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:SAB2554c
    OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
    Taxonomic identifieri273036 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000001927: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Histidinol dehydrogenasePRO_0000229866Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi273036.SAB2554c.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2YZB4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiICGPGNK.
    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.

    Q2YZB4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNAQQFLNQ FSLEAPLDES LYPIIRDICQ EVKVHGDKAL KMYNLTFDHT    50
    KTDHLEISHE QIKAAFDTLD EKTKQALQQS YERIKAYQES IKQTNQQLEK 100
    SVECYEIYHP LESVGIYVPG GKASYPSTVL MTATLAQVAG VENIVVVTPP 150
    QPNGVSQEVL AACYITQVNQ VFQVGGAQSI AALTYGTETI PKVDKIVGPG 200
    NQFVAYAKKY LFGQVGIDQI AGPTEIALII DDTADLDAIV YDVFAQAEHD 250
    ELARTYVISE DAQVLKDLES RITKALPNVD RYDIVSKSIA NQHYLIHASN 300
    FDDACHVMNT IAPEHASIQT VNPQPYIEKV KYVGALFIGH YSPEVIGDYV 350
    AGPSHVLPTN RTARFTNGLS VNDFLTRNTV IHLSKDTFEQ IADSAQHIAH 400
    VEALYNHQQS ILIRQS 416
    Length:416
    Mass (Da):46,206
    Last modified:December 20, 2005 - v1
    Checksum:iD05A097D8E2860C5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ938182 Genomic DNA. Translation: CAI82242.1.
    RefSeqiYP_417997.1. NC_007622.1.

    Genome annotation databases

    EnsemblBacteriaiCAI82242; CAI82242; SAB2554c.
    GeneIDi3794915.
    KEGGisab:SAB2554c.
    PATRICi19526193. VBIStaAur92441_2692.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ938182 Genomic DNA. Translation: CAI82242.1 .
    RefSeqi YP_417997.1. NC_007622.1.

    3D structure databases

    ProteinModelPortali Q2YZB4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273036.SAB2554c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAI82242 ; CAI82242 ; SAB2554c .
    GeneIDi 3794915.
    KEGGi sab:SAB2554c.
    PATRICi 19526193. VBIStaAur92441_2692.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci SAUR273036:GJVS-2627-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. "Molecular correlates of host specialization in Staphylococcus aureus."
      Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
      PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: bovine RF122 / ET3-1.

    Entry informationi

    Entry nameiHISX_STAAB
    AccessioniPrimary (citable) accession number: Q2YZB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 66 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3