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P07685

- HIS2_NEUCR

UniProt

P07685 - HIS2_NEUCR

Protein

Histidine biosynthesis trifunctional protein

Gene

his-3

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      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 bindingi693 – 6931ZincBy similarity
    Metal bindingi696 – 6961ZincBy similarity
    Active sitei762 – 7621By similarity
    Active sitei763 – 7631By similarity
    Metal bindingi796 – 7961ZincBy similarity
    Metal bindingi855 – 8551ZincBy 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

    SABIO-RKP07685.
    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:his-3
    ORF Names:5C2.120, NCU03139
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 1, Linkage Group I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870Histidine biosynthesis trifunctional proteinPRO_0000135911Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5141.NCU03139.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP07685.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 285285Phosphoribosyl-AMP cyclohydrolaseAdd
    BLAST
    Regioni286 – 36782Phosphoribosyl-ATP pyrophosphohydrolaseAdd
    BLAST
    Regioni368 – 870503Histidinol 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.

    P07685-1 [UniParc]FASTAAdd to Basket

    « Hide

    METTLPLPFL VGVSVPPGLN DIKEGLSREE VSCLGCVFFE VKPQTLEKIL    50
    RFLKRHNVEF EPYFDVTALE SIDDIITLLD AGARKVFVKT EQLADLSAYG 100
    SRVAPIVTGS SAALLSSATE SGLLLSGFDQ TASEAAQFLE EARDKKITPF 150
    FIKPVPGADL EQFIQVAAKA NAIPILPSTG LTTKKDEAGK LAISTILSSV 200
    WKSDRPDGLL PTVVVDEHDT ALGLVYSSAE SVNEALRTQT GVYQSRKRGL 250
    WYKGATSGDT QELVRISLDC DNDALKFVVK QKGRFCHLDQ SGCFGQLKGL 300
    PKLEQTLISR KQSAPEGSYT ARLFSDEKLV RAKIMEEAEE LCTAQTPQEI 350
    AFEAADLFYF ALTRAVAAGV TLADIERSLD AKSWKVKRRT GDAKGKWAEK 400
    EGIKPAASAL AATSAPVTKE AAQETTPEKI TMRRFDASKV STEELDAALK 450
    RPAQKSSDAI YKIIVPIIED VRKNGDKAVL SYTHKFEKAT SLTSPVLKAP 500
    FPKELMQLPE ETIAAIDVSF ENIRKFHAAQ KEEKPLQVET MPGVVCSRFS 550
    RPIEAVGCYI PGGTAVLPST ALMLGVPAMV AGCNKIVFAS PPRADGTITP 600
    EIVYVAHKVG AESIVLAGGA QAVAAMAYGT ESITKVDKIL GPGNQFVTAA 650
    KMFVSNDTNA AVGIDMPAGP SEVLVIADKD ANPAFVASDL LSQAEHGVDS 700
    QVILIAIDLD EEHLQAIEDE VHRQATELPR VQIVRGSIAH SITVQVKTVE 750
    EAMELSNKYA PEHLILQIKE AEKAVDLVMN AGSVFIGAWT PESVGDYSAG 800
    VNHSLPTYGF AKQYSGVNLA SFVKHITSSN LTAEGLKNVG QAVMQLAKVE 850
    ELEAHRRAVS IRLEHMSKSN 870
    Length:870
    Mass (Da):93,836
    Last modified:June 7, 2005 - v3
    Checksum:iACE28C977682E120
    GO

    Sequence cautioni

    The sequence AAA33588.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti604 – 6041Y → H in AAC02221. 1 PublicationCurated
    Sequence conflicti604 – 6041Y → H in AAC02222. 1 PublicationCurated
    Sequence conflicti811 – 8111A → G in AAC02221. 1 PublicationCurated
    Sequence conflicti811 – 8111A → G in AAC02222. 1 PublicationCurated
    Sequence conflicti819 – 8191L → F in AAC02221. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441Q → K in strain: FGSC 541. 1 Publication
    Natural varianti50 – 501L → V in strain: FGSC 541. 1 Publication
    Natural varianti410 – 4101L → P in strain: FGSC 541. 1 Publication
    Natural varianti708 – 7081D → N in strain: FGSC 541. 1 Publication
    Natural varianti726 – 7261T → M in strain: FGSC 541. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27531 Genomic DNA. Translation: AAA33588.1. Frameshift.
    AF045455 Genomic DNA. Translation: AAC02221.1.
    AF045456 Genomic DNA. Translation: AAC02222.1.
    BX842637 Genomic DNA. Translation: CAE76555.1.
    CM002236 Genomic DNA. Translation: EAA34952.1.
    PIRiA23978. SHNC.
    RefSeqiXP_964188.1. XM_959095.2.
    UniGeneiNcr.7165.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000002825; EFNCRP00000002825; EFNCRG00000002822.
    GeneIDi3880337.
    KEGGincr:NCU03139.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27531 Genomic DNA. Translation: AAA33588.1 . Frameshift.
    AF045455 Genomic DNA. Translation: AAC02221.1 .
    AF045456 Genomic DNA. Translation: AAC02222.1 .
    BX842637 Genomic DNA. Translation: CAE76555.1 .
    CM002236 Genomic DNA. Translation: EAA34952.1 .
    PIRi A23978. SHNC.
    RefSeqi XP_964188.1. XM_959095.2.
    UniGenei Ncr.7165.

    3D structure databases

    ProteinModelPortali P07685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU03139.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000002825 ; EFNCRP00000002825 ; EFNCRG00000002822 .
    GeneIDi 3880337.
    KEGGi ncr:NCU03139.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00007 .
    UPA00031 ; UER00008 .
    UPA00031 ; UER00014 .
    SABIO-RK P07685.

    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. "Cloning and characterization of the multifunctional his-3 gene of Neurospora crassa."
      Legerton T.L., Yanofsky C.
      Gene 39:129-140(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 74-OR23-1VA / FGSC 2489.
    2. "DNA sequence of histidine-3 from two Neurospora wild-types."
      Yeadon P.J., Petersen A., Catcheside D.E.A.
      Fungal Genet. Newsl. 45:43-43(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-44; VAL-50; PRO-410; ASN-708 AND MET-726.
      Strain: 74-OR23-1VA / FGSC 2489 and FGSC 541.
    3. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    4. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiHIS2_NEUCR
    AccessioniPrimary (citable) accession number: P07685
    Secondary accession number(s): O42788, O42789, Q7RVK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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