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Protein

Cyanide hydratase

Gene

chy1

Organism
Gibberella baccata (Fusarium lateritium)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants (PubMed:8409923). Has also low but significant nitrilase activity with acetonitrile, propionitrile and benzonitrile (PubMed:12725921).2 Publications

Catalytic activityi

Formamide = cyanide + H2O.1 Publication

Kineticsi

  1. KM=43 mM for cyanide1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei46Proton acceptor1
    Active sitei1281
    Active sitei163Nucleophile1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase, Lyase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanide hydratase1 Publication (EC:4.2.1.661 Publication)
    Short name:
    CHT
    Alternative name(s):
    Cyanide-degrading nitrilase
    Formamide hydrolyase1 Publication
    Gene namesi
    Name:chy11 Publication
    OrganismiGibberella baccata (Fusarium lateritium)
    Taxonomic identifieri5523 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium lateritium species complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi163C → A: Completely abolishes enzymatic activity. 1 Publication1
    Mutagenesisi170F → L: Completely abolishes enzymatic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002040471 – 355Cyanide hydrataseAdd BLAST355

    Expressioni

    Inductioni

    By cyanide.1 Publication

    Interactioni

    Subunit structurei

    Oligomer of dimers, forming left-handed helical fibers.

    Structurei

    3D structure databases

    ProteinModelPortaliP32963.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini6 – 286CN hydrolaseAdd BLAST281

    Sequence similaritiesi

    Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.Curated

    Family and domain databases

    Gene3Di3.60.110.10. 1 hit.
    HAMAPiMF_03224. CN_hydrolase. 1 hit.
    InterProiView protein in InterPro
    IPR003010. C-N_Hydrolase.
    IPR036526. C-N_Hydrolase_sf.
    IPR000132. Nitrilase/CN_hydratase_CS.
    PfamiView protein in Pfam
    PF00795. CN_hydrolase. 1 hit.
    SUPFAMiSSF56317. SSF56317. 1 hit.
    PROSITEiView protein in PROSITE
    PS50263. CN_HYDROLASE. 1 hit.
    PS00920. NITRIL_CHT_1. 1 hit.
    PS00921. NITRIL_CHT_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32963-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAITKYKAAA VTSEPGWFDL EGGVRKTIDF INEAGEAGCK FVAFPEVWIP
    60 70 80 90 100
    GYPYWMWKVT YLQSLPMLKR YRENSMAVDS EEMRRIRRAA RDNQIFVSLG
    110 120 130 140 150
    FSEIDHATLY LSQVLIGPDG AVINHRRKIK PTHVEKLVYG DGSGDTFMSV
    160 170 180 190 200
    SETEIGRVGQ LNCWENMNPF LKSLNVSAGE QVHVAAWPVY PGKERQVHPD
    210 220 230 240 250
    PATNYADPAS DLVTPEYAIE TGTWTLAPFQ RLSVEGLKIN TPEGVEPETD
    260 270 280 290 300
    PSVYNGHARI YRPDGSLVVK PEKDFDGLLF VDIDLNECHL TKVLADFAGH
    310 320 330 340 350
    YMRPDLIRLL VDTRRKKLIT EADPNGSIAT YSTRQRLGLD KPLSKKEGDE

    TTDVL
    Length:355
    Mass (Da):39,879
    Last modified:May 10, 2017 - v2
    Checksum:iB6304651F5360B5D
    GO

    Sequence cautioni

    The sequence AAA33336 differs from that shown. Reason: Frameshift at positions 122, 132, 159, 193, 235 and 341.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M99046 mRNA. Translation: AAA33336.1. Frameshift.

    Similar proteinsi

    Entry informationi

    Entry nameiCHT_GIBBA
    AccessioniPrimary (citable) accession number: P32963
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 10, 2017
    Last modified: October 25, 2017
    This is version 66 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families