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O13471

- HIS2_KLULA

UniProt

O13471 - HIS2_KLULA

Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (27 Sep 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 bindingi614 – 6141ZincBy similarity
    Metal bindingi617 – 6171ZincBy similarity
    Active sitei683 – 6831By similarity
    Active sitei684 – 6841By similarity
    Metal bindingi717 – 7171ZincBy similarity
    Metal bindingi776 – 7761ZincBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-UniPathway

    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

    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:KLLA0C01452g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome C

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 795795Histidine biosynthesis trifunctional proteinPRO_0000135910Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi28985.O13471.

    Structurei

    3D structure databases

    ProteinModelPortaliO13471.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 225225Phosphoribosyl-AMP cyclohydrolaseAdd
    BLAST
    Regioni226 – 30883Phosphoribosyl-ATP pyrophosphohydrolaseAdd
    BLAST
    Regioni309 – 795487Histidinol 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.

    O13471-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI    50
    SVLLKDAKFE DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK 100
    DGAYQFSFGQ IQEIQQSQLV KASEISLETF TNSVLSGMKT DRPDGLYTTL 150
    VVDENERSLG LVYSNKESVS LAIETQTGIY FSRSRNEIWR KGATSGNVQK 200
    LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG LYGLQKLLQE 250
    RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY 300
    FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED 350
    GKIVLNVVSA SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV 400
    ELTAKFDGVQ LETPVLEAPY PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ 450
    MQSETLDVET QPGVVCSRFP RPIEKVGLYI PGGTAILPST ALMLGVPAQV 500
    AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG AQAIAAMAYG 550
    TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE 600
    EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP 650
    RVDIVRKCIA HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD 700
    HAGSIFVGAY TPESCGDYSS GTNHTLPTYG YARQYSGVNT ATFQKFITSQ 750
    VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV KIRMSKLGLL PSGFE 795
    Length:795
    Mass (Da):86,795
    Last modified:September 27, 2004 - v2
    Checksum:i6D35F1632280D3B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1632VY → DI in CAA70698. (PubMed:9639316)Curated
    Sequence conflicti580 – 5823QAL → LAI in CAA70698. (PubMed:9639316)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09503 Genomic DNA. Translation: CAA70698.1.
    CR382123 Genomic DNA. Translation: CAH01111.1.
    RefSeqiXP_452260.1. XM_452260.1.

    Genome annotation databases

    GeneIDi2892606.
    KEGGikla:KLLA0C01452g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09503 Genomic DNA. Translation: CAA70698.1 .
    CR382123 Genomic DNA. Translation: CAH01111.1 .
    RefSeqi XP_452260.1. XM_452260.1.

    3D structure databases

    ProteinModelPortali O13471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.O13471.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2892606.
    KEGGi kla:KLLA0C01452g.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00007 .
    UPA00031 ; UER00008 .
    UPA00031 ; UER00014 .

    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 HIS4 gene from the yeast Kluyveromyces lactis."
      Freire-Picos M.A., Hampsey M., Cerdan M.E.
      Yeast 14:687-691(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiHIS2_KLULA
    AccessioniPrimary (citable) accession number: O13471
    Secondary accession number(s): Q6CUX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3