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Protein

Cyanide hydratase

Gene

cht

Organism
Microdochium sorghi (Zonate leaf spot disease fungus) (Gloeocercospora sorghi)
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.UniRule annotation1 Publication

Catalytic activityi

Formamide = cyanide + H2O.UniRule annotation1 Publication

Kineticsi

  1. KM=12 mM for cyanide (at pH 8 and 25 degrees Celsium)1 Publication
  2. KM=90 mM for cyanide (at pH 7.8 and 23 degrees Celsium)1 Publication
  1. Vmax=4.4 mmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7-8 (PubMed:1416986, PubMed:15703908). Active from pH 6 to pH 8.5 (PubMed:15703908, PubMed:18587571).3 Publications

Temperature dependencei

Optimum temperature is 42-55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei46Proton acceptorUniRule annotation1
Active sitei128UniRule annotation1
Active sitei163NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17777.
BRENDAi4.2.1.66. 2449.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyanide hydratase1 PublicationUniRule annotation (EC:4.2.1.66UniRule annotation1 Publication)
Short name:
CHT1 PublicationUniRule annotation
Alternative name(s):
Cyanide-degrading nitrilaseUniRule annotation
Formamide hydrolyaseUniRule annotation
Gene namesi
Name:cht1 Publication
OrganismiMicrodochium sorghi (Zonate leaf spot disease fungus) (Gloeocercospora sorghi)
Taxonomic identifieri1682391 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesXylariomycetidaeXylarialesMicrodochiaceaeMicrodochium

Pathology & Biotechi

Disruption phenotypei

Highly sensitive to cyanide, but retains virulence on sorghum.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002040481 – 368Cyanide hydrataseAdd BLAST368

Expressioni

Inductioni

By cyanide.UniRule annotation

Interactioni

Subunit structurei

Oligomer of dimers, forming left-handed helical fibers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP32964.
SMRiP32964.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 285CN hydrolasePROSITE-ProRule annotationAdd BLAST280

Sequence similaritiesi

Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.UniRule annotationCurated

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.

P32964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPINKYKAAV VTSEPVWENL EGGVVKTIEF INEAGKAGCK LIAFPEVWIP
60 70 80 90 100
GYPYWMWKVN YLQSLPMLKA YRENSIAMDS SEMRRIRAAA RDNQIYVSIG
110 120 130 140 150
VSEIDHATLY LTQVLISPLG DVINHRRKIK PTHVEKLVYG DGSGDSFEPV
160 170 180 190 200
TQTEIGRLGQ LNCWENMNPF LKSLAVARGE QIHVAAWPVY PDLSKQVHPD
210 220 230 240 250
PATNYADPAS DLVTPAYAIE TGTWVLAPFQ RISVEGLKRH TPPGVEPETD
260 270 280 290 300
ATPYNGHARI FRPDGSLYAK PAVDFDGLMY VDIDLNESHL TKALADFAGH
310 320 330 340 350
YMRPDLIRLL VDTRRKELVT EVGGGDNGGI QSYSTMARLG LDRPLEEEDY
360
RQGTDAGETE KASSNGHA
Length:368
Mass (Da):40,899
Last modified:October 1, 1993 - v1
Checksum:i5A03113E515A3575
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99044 Genomic DNA. Translation: AAA33353.1.
PIRiJQ1613.

Similar proteinsi

Entry informationi

Entry nameiCHT_MICSH
AccessioniPrimary (citable) accession number: P32964
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 25, 2017
This is version 71 of the entry and version 1 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