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Q12670

- HIS2_SACBA

UniProt

Q12670 - HIS2_SACBA

Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces eubayanus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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: 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
    OrganismiSaccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces eubayanus)
    Taxonomic identifieri4931 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 799799Histidine biosynthesis trifunctional proteinPRO_0000135913Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ12670.
    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

    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.

    Q12670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP    50
    LVALSLPNAK FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR 100
    IVVEGNGVFH NQFLVNQKFS QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG 150
    LFTTLVVDQY ERCLGLVYSS KESIAKAIDL GRGVYYSRSR NEIWVKGETS 200
    GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE FKHGLVGLES 250
    LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA 300
    DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE 350
    EAPTGPIHLH VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD 400
    SALLEYTEKF DGVKLSTPVL NAPFPEEYFE GLTEEMKDAL DLSIENVRKF 450
    HAAQLPKETL EVETQPGVLC SRFPRPIEKV GLYIPGGTAI LPSTALMLGV 500
    PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV LAGGAQAVAA 550
    MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 600
    IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA 650
    MQLPRVDIVR KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV 700
    KLVDNAGSVF VGAYTPESCG DYSSGTNHTL PTYGYARQYS GANTATFQKF 750
    ITAQNITPEG LENIGRAVMC VAKKEGLDGH RNAVKIRMSK LGLIPKDFQ 799
    Length:799
    Mass (Da):87,734
    Last modified:November 1, 1996 - v1
    Checksum:i35793E26EDB81B6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13062 Genomic DNA. Translation: AAA21153.1.
    AJ251575 Genomic DNA. Translation: CAC16411.1.
    PIRiS53349.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13062 Genomic DNA. Translation: AAA21153.1 .
    AJ251575 Genomic DNA. Translation: CAC16411.1 .
    PIRi S53349.

    3D structure databases

    ProteinModelPortali Q12670.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 polyfunctional HIS4 gene of Saccharomyces carlsbergensis: sequence and homology analysis."
      Porter G.L.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the constitution of the beer yeast genome by PCR, sequencing and subtelomeric sequence hybridization."
      Casaregola S., Nguyen H.V., Lapathitis G., Kotyk A., Gaillardin C.
      Int. J. Syst. Evol. Microbiol. 51:1607-1618(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
      Strain: ATCC 76513 / CBS 380 / DSM 70412 / JCM 7258 / NBRC 1127 / NRRL Y-12624.

    Entry informationi

    Entry nameiHIS2_SACBA
    AccessioniPrimary (citable) accession number: Q12670
    Secondary accession number(s): Q9HFG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

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

    External Data

    Dasty 3