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Q8ZFX5

- HISX_YERPE

UniProt

Q8ZFX5 - HISX_YERPE

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Yersinia pestis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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 sitei133 – 1331NADUniRule annotation
    Binding sitei191 – 1911NADUniRule annotation
    Binding sitei214 – 2141NADUniRule annotation
    Binding sitei240 – 2401SubstrateUniRule annotation
    Metal bindingi262 – 2621ZincUniRule annotation
    Binding sitei262 – 2621SubstrateUniRule annotation
    Metal bindingi265 – 2651ZincUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule 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

    BioCyciYPES214092:GKDD-1529-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:YPO1548, y2621, YP_1437
    OrganismiYersinia pestis
    Taxonomic identifieri632 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000000815: Chromosome, UP000001019: Chromosome, UP000002490: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Histidinol dehydrogenasePRO_0000135887Add
    BLAST

    Proteomic databases

    PRIDEiQ8ZFX5.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ8ZFX5. 10 interactions.
    STRINGi214092.YPO1548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8ZFX5.
    SMRiQ8ZFX5. Positions 5-433.
    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.

    Q8ZFX5-1 [UniParc]FASTAAdd to Basket

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    MQPTNFNTLI NWQQCSEEQQ KALLSRPAIN ASERITAAVS DILDRVKAEG    50
    DSALRDFSQR FDHVQVADIR ITASEIAAAS ARLSDDVKHA MAQAVRNIEI 100
    FHNAQKMPVV DVETQPGVRC QQITRPIASV GLYIPGGSAP LPSTVLMLGT 150
    PARIAGCQRV VLCSPPPIAD EILYAAQLCG IQEVFQIGGA QAIAAMAFGS 200
    ESVPKVHKIF GPGNAYVTEA KRQVSQRLDG AAIDMPAGPS EVLVIADSGA 250
    TPAFIAADLL SQAEHGPDSQ VILLTPDAAI AQAVAVEVEQ QLALLSRADI 300
    ARQALESSRL IVTNDLQQCI DISNAYGPEH LILQIRQPEE IIDQIDNAGS 350
    VFMGDWSPES AGDYASGTNH VLPTYGYTST YSSLGLADFV KRMTVQQLTP 400
    QGLLGLASTI ETLAQAEQLT AHKNAVTLRV TALNNALTAV NKE 443
    Length:443
    Mass (Da):47,233
    Last modified:March 1, 2002 - v1
    Checksum:iE4841C0ACE54772C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590842 Genomic DNA. Translation: CAL20194.1.
    AE009952 Genomic DNA. Translation: AAM86175.1.
    AE017042 Genomic DNA. Translation: AAS61678.1.
    PIRiAH0188.
    RefSeqiNP_669924.1. NC_004088.1.
    NP_992801.1. NC_005810.1.
    YP_002346564.1. NC_003143.1.

    Genome annotation databases

    EnsemblBacteriaiAAM86175; AAM86175; y2621.
    AAS61678; AAS61678; YP_1437.
    GeneIDi1147568.
    1174387.
    2765680.
    KEGGiype:YPO1548.
    ypk:y2621.
    ypm:YP_1437.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590842 Genomic DNA. Translation: CAL20194.1 .
    AE009952 Genomic DNA. Translation: AAM86175.1 .
    AE017042 Genomic DNA. Translation: AAS61678.1 .
    PIRi AH0188.
    RefSeqi NP_669924.1. NC_004088.1.
    NP_992801.1. NC_005810.1.
    YP_002346564.1. NC_003143.1.

    3D structure databases

    ProteinModelPortali Q8ZFX5.
    SMRi Q8ZFX5. Positions 5-433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8ZFX5. 10 interactions.
    STRINGi 214092.YPO1548.

    Proteomic databases

    PRIDEi Q8ZFX5.

    Protocols and materials databases

    DNASUi 1147568.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM86175 ; AAM86175 ; y2621 .
    AAS61678 ; AAS61678 ; YP_1437 .
    GeneIDi 1147568.
    1174387.
    2765680.
    KEGGi ype:YPO1548.
    ypk:y2621.
    ypm:YP_1437.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .
    BioCyci YPES214092:GKDD-1529-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CO-92 / Biovar Orientalis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KIM10+ / Biovar Mediaevalis.
    3. "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
      Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R.
      , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
      DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 91001 / Biovar Mediaevalis.

    Entry informationi

    Entry nameiHISX_YERPE
    AccessioniPrimary (citable) accession number: Q8ZFX5
    Secondary accession number(s): Q0WGM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 95 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