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Q9P777

- HISX_SCHPO

UniProt

Q9P777 - HISX_SCHPO

Protein

Histidinol dehydrogenase

Gene

his2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.By similarity

    Catalytic activityi

    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei132 – 1321NADBy similarity
    Binding sitei194 – 1941NADBy similarity
    Binding sitei217 – 2171NADBy similarity
    Binding sitei244 – 2441SubstrateBy similarity
    Metal bindingi266 – 2661ZincBy similarity
    Binding sitei266 – 2661SubstrateBy similarity
    Metal bindingi269 – 2691ZincBy similarity
    Binding sitei269 – 2691SubstrateBy similarity
    Active sitei335 – 3351Proton acceptorBy similarity
    Active sitei336 – 3361Proton acceptorBy similarity
    Binding sitei336 – 3361SubstrateBy similarity
    Metal bindingi369 – 3691ZincBy similarity
    Binding sitei369 – 3691SubstrateBy similarity
    Binding sitei423 – 4231SubstrateBy similarity
    Metal bindingi428 – 4281ZincBy similarity
    Binding sitei428 – 4281SubstrateBy similarity

    GO - Molecular functioni

    1. histidinol dehydrogenase activity Source: PomBase
    2. NAD binding Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histidine biosynthetic process Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:his2
    ORF Names:SPBC1711.13
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC1711.13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Histidinol dehydrogenasePRO_0000135908Add
    BLAST

    Proteomic databases

    MaxQBiQ9P777.
    PaxDbiQ9P777.

    Interactioni

    Protein-protein interaction databases

    BioGridi276205. 5 interactions.
    DIPiDIP-59120N.
    MINTiMINT-4704831.
    STRINGi4896.SPBC1711.13-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK00013.
    OMAiPRGDFAS.
    OrthoDBiEOG7DJSVM.
    PhylomeDBiQ9P777.

    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.

    Q9P777-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEYEIQVPS YRAAALTAEE RTRLLARPIQ NTQKIRTIVQ PIIEDVKSRG    50
    EASLIDYASK FEKVQLKSAV LKAPFDDDLM KISPMIKEDI DIAFNNIFAF 100
    HSSQLRPTIA VQTMRGVVCQ RMSRPINRVG LYIPGGTAVL PSTALMLGVP 150
    AKVAGCPHVV ISTPVRKDGT VAPEIVYIAN KIGAEAIILA GGAQAIAAMA 200
    YGISGVPKVN KIFGPGNQFV TAAKMHVQND YGALVAIDLP AGPSEVLVIA 250
    DETCNPESVA LDLLSQAEHG LDSQIILLTV SLSPEMFDRI QKAINDHALR 300
    LSRSYIIKHA IKKSVIVQVD NVDQAFEWSN LYGPEHLVLH LKNASSYIPK 350
    IDNAGSVFVG PWSPVSMGDY ASGTNHTLPT YGYASSYSGV STDSFLKYIT 400
    TQELTEEGIQ RLGPTVIRLA ELEGLTAHAD AVRVRGVRL 439
    Length:439
    Mass (Da):47,554
    Last modified:October 1, 2000 - v1
    Checksum:i7B054B5DBDAB2DEA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB88243.1.
    RefSeqiNP_595886.1. NM_001021792.2.

    Genome annotation databases

    EnsemblFungiiSPBC1711.13.1; SPBC1711.13.1:pep; SPBC1711.13.
    GeneIDi2539650.
    KEGGispo:SPBC1711.13.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB88243.1 .
    RefSeqi NP_595886.1. NM_001021792.2.

    3D structure databases

    ProteinModelPortali Q9P777.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276205. 5 interactions.
    DIPi DIP-59120N.
    MINTi MINT-4704831.
    STRINGi 4896.SPBC1711.13-1.

    Proteomic databases

    MaxQBi Q9P777.
    PaxDbi Q9P777.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC1711.13.1 ; SPBC1711.13.1:pep ; SPBC1711.13 .
    GeneIDi 2539650.
    KEGGi spo:SPBC1711.13.

    Organism-specific databases

    PomBasei SPBC1711.13.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K00013.
    OMAi PRGDFAS.
    OrthoDBi EOG7DJSVM.
    PhylomeDBi Q9P777.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00014 .

    Miscellaneous databases

    NextBioi 20800804.
    PROi Q9P777.

    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 Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiHISX_SCHPO
    AccessioniPrimary (citable) accession number: Q9P777
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 28, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    In contrast to other fungi who have a single histidine biosynthesis trifunctional protein, 2 proteins are present in S.pombe to ensure these functions: his7 (phosphoribosyl-AMP cyclohydrolase and phosphoribosyl-ATP pyrophosphatase activities) and his2 (histidinol dehydrogenase activity).Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3