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P00815

- HIS2_YEAST

UniProt

P00815 - HIS2_YEAST

Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (29 Mar 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.
    1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
    L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

    Cofactori

    Binds 1 zinc ion.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi618 – 6181ZincBy similarity
    Metal bindingi621 – 6211ZincBy similarity
    Active sitei687 – 6871By similarity
    Active sitei688 – 6881By similarity
    Metal bindingi721 – 7211ZincBy similarity
    Metal bindingi780 – 7801ZincBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histidinol dehydrogenase activity Source: SGD
    3. NAD binding Source: InterPro
    4. phosphoribosyl-AMP cyclohydrolase activity Source: SGD
    5. phosphoribosyl-ATP diphosphatase activity Source: SGD
    6. protein binding Source: IntAct
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histidine biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YCL030C-MONOMER.
    UniPathwayiUPA00031; UER00007.
    UPA00031; UER00008.
    UPA00031; UER00014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine biosynthesis trifunctional protein
    Including the following 3 domains:
    Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
    Phosphoribosyl-ATP pyrophosphohydrolase (EC:3.6.1.31)
    Histidinol dehydrogenase (EC:1.1.1.23)
    Short name:
    HDH
    Gene namesi
    Name:HIS4
    Ordered Locus Names:YCL030C
    ORF Names:YCL183, YCL30C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCL030c.
    SGDiS000000535. HIS4.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 799799Histidine biosynthesis trifunctional proteinPRO_0000135914Add
    BLAST

    Proteomic databases

    MaxQBiP00815.
    PaxDbiP00815.
    PeptideAtlasiP00815.

    Expressioni

    Gene expression databases

    GenevestigatoriP00815.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FMP48P532332EBI-8334,EBI-9664

    Protein-protein interaction databases

    BioGridi30953. 25 interactions.
    DIPiDIP-6402N.
    IntActiP00815. 14 interactions.
    MINTiMINT-617364.
    STRINGi4932.YCL030C.

    Structurei

    3D structure databases

    ProteinModelPortaliP00815.
    SMRiP00815. Positions 164-238, 356-791.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229Phosphoribosyl-AMP cyclohydrolaseAdd
    BLAST
    Regioni230 – 31283Phosphoribosyl-ATP pyrophosphohydrolaseAdd
    BLAST
    Regioni313 – 799487Histidinol dehydrogenaseAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the histidinol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG0141.
    HOGENOMiHOG000243914.
    KOiK14152.
    OMAiNIRKFHA.
    OrthoDBiEOG7DJSVM.

    Family and domain databases

    HAMAPiMF_01024. HisD.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016298. Histidine_synth_trifunct.
    IPR001692. Histidinol_DH_CS.
    IPR012131. Hstdl_DH.
    IPR008179. PRib-ATP_PPHydrolase.
    IPR021130. PRib-ATP_PPHydrolase-like.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view]
    PfamiPF00815. Histidinol_dh. 1 hit.
    PF01502. PRA-CH. 1 hit.
    PF01503. PRA-PH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001257. His_trifunctional. 1 hit.
    PRINTSiPR00083. HOLDHDRGNASE.
    ProDomiPD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR00069. hisD. 1 hit.
    TIGR03188. histidine_hisI. 1 hit.
    PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00815-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLPILPLID DLASWNSKKE YVSLVGQVLL DGSSLSNEEI LQFSKEEEVP    50
    LVALSLPSGK FSDDEIIAFL NNGVSSLFIA SQDAKTAEHL VEQLNVPKER 100
    VVVEENGVFS NQFMVKQKFS QDKIVSIKKL SKDMLTKEVL GEVRTDRPDG 150
    LYTTLVVDQY ERCLGLVYSS KKSIAKAIDL GRGVYYSRSR NEIWIKGETS 200
    GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE FKHGLVGLES 250
    LLKQRLQDAP EESYTRRLFN DSALLDAKIK EEAEELTEAK GKKELSWEAA 300
    DLFYFALAKL VANDVSLKDV ENNLNMKHLK VTRRKGDAKP KFVGQPKAEE 350
    EKLTGPIHLD VVKASDKVGV QKALSRPIQK TSEIMHLVNP IIENVRDKGN 400
    SALLEYTEKF DGVKLSNPVL NAPFPEEYFE GLTEEMKEAL DLSIENVRKF 450
    HAAQLPTETL EVETQPGVLC SRFPRPIEKV GLYIPGGTAI LPSTALMLGV 500
    PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGASKIV LAGGAQAVAA 550
    MAYGTETIPK VDKILGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 600
    IADEDADVDF VASDLLSQAE HGIDSQVILV GVNLSEKKIQ EIQDAVHNQA 650
    LQLPRVDIVR KCIAHSTIVL CDGYEEALEM SNQYAPEHLI LQIANANDYV 700
    KLVDNAGSVF VGAYTPESCG DYSSGTNHTL PTYGYARQYS GANTATFQKF 750
    ITAQNITPEG LENIGRAVMC VAKKEGLDGH RNAVKIRMSK LGLIPKDFQ 799
    Length:799
    Mass (Da):87,721
    Last modified:March 29, 2004 - v3
    Checksum:i0B82D289BEAB754D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531A → R in CAA24617. (PubMed:7049842)Curated
    Sequence conflicti386 – 3861H → Y in CAA24617. (PubMed:7049842)Curated
    Sequence conflicti402 – 4032AL → VF in CAA24617. (PubMed:7049842)Curated
    Sequence conflicti441 – 4411D → N in CAA24617. (PubMed:7049842)Curated
    Sequence conflicti794 – 7941I → F in CAA24617. (PubMed:7049842)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01310 Genomic DNA. Translation: CAA24617.1.
    X59720 Genomic DNA. Translation: CAA42355.2.
    V01309 Genomic DNA. Translation: CAA24616.1.
    M11491 Genomic DNA. Translation: AAA67504.1.
    M11492 Genomic DNA. Translation: AAA67505.1.
    M11694 Unassigned DNA. Translation: AAA18400.1.
    M11695 Unassigned DNA. Translation: AAA18401.1.
    M11696 Unassigned DNA. Translation: AAA18402.1.
    BK006937 Genomic DNA. Translation: DAA07454.1.
    PIRiS17473. SHBY.
    RefSeqiNP_009900.2. NM_001178675.1.

    Genome annotation databases

    EnsemblFungiiYCL030C; YCL030C; YCL030C.
    GeneIDi850327.
    KEGGisce:YCL030C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01310 Genomic DNA. Translation: CAA24617.1 .
    X59720 Genomic DNA. Translation: CAA42355.2 .
    V01309 Genomic DNA. Translation: CAA24616.1 .
    M11491 Genomic DNA. Translation: AAA67504.1 .
    M11492 Genomic DNA. Translation: AAA67505.1 .
    M11694 Unassigned DNA. Translation: AAA18400.1 .
    M11695 Unassigned DNA. Translation: AAA18401.1 .
    M11696 Unassigned DNA. Translation: AAA18402.1 .
    BK006937 Genomic DNA. Translation: DAA07454.1 .
    PIRi S17473. SHBY.
    RefSeqi NP_009900.2. NM_001178675.1.

    3D structure databases

    ProteinModelPortali P00815.
    SMRi P00815. Positions 164-238, 356-791.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 30953. 25 interactions.
    DIPi DIP-6402N.
    IntActi P00815. 14 interactions.
    MINTi MINT-617364.
    STRINGi 4932.YCL030C.

    Proteomic databases

    MaxQBi P00815.
    PaxDbi P00815.
    PeptideAtlasi P00815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCL030C ; YCL030C ; YCL030C .
    GeneIDi 850327.
    KEGGi sce:YCL030C.

    Organism-specific databases

    CYGDi YCL030c.
    SGDi S000000535. HIS4.

    Phylogenomic databases

    eggNOGi COG0141.
    HOGENOMi HOG000243914.
    KOi K14152.
    OMAi NIRKFHA.
    OrthoDBi EOG7DJSVM.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00007 .
    UPA00031 ; UER00008 .
    UPA00031 ; UER00014 .
    BioCyci YEAST:YCL030C-MONOMER.

    Miscellaneous databases

    NextBioi 965751.

    Gene expression databases

    Genevestigatori P00815.

    Family and domain databases

    HAMAPi MF_01024. HisD.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016298. Histidine_synth_trifunct.
    IPR001692. Histidinol_DH_CS.
    IPR012131. Hstdl_DH.
    IPR008179. PRib-ATP_PPHydrolase.
    IPR021130. PRib-ATP_PPHydrolase-like.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view ]
    Pfami PF00815. Histidinol_dh. 1 hit.
    PF01502. PRA-CH. 1 hit.
    PF01503. PRA-PH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001257. His_trifunctional. 1 hit.
    PRINTSi PR00083. HOLDHDRGNASE.
    ProDomi PD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR00069. hisD. 1 hit.
    TIGR03188. histidine_hisI. 1 hit.
    PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of the HIS4 region of yeast."
      Donahue T.F., Farabaugh P.J., Fink G.R.
      Gene 18:47-59(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames."
      Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.
      Yeast 7:533-538(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 375.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair duplication."
      Farabaugh P.J., Fink G.R.
      Nature 286:352-356(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
    7. "Transposable element sequences involved in the enhancement of yeast gene expression."
      Roeder G.S., Rose A.B., Pearlman R.E.
      Proc. Natl. Acad. Sci. U.S.A. 82:5428-5432(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHIS2_YEAST
    AccessioniPrimary (citable) accession number: P00815
    Secondary accession number(s): D6VQY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 29, 2004
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 521 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3