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Protein

Cyanide hydratase

Gene
N/A
Organism
Aspergillus niger
Status
Reviewed-Annotation score: -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:23475593, Ref. 5). Can also transform some nitriles like 2-cyanopyridine and fumaronitrile (Ref. 5).UniRule annotation2 Publications

Catalytic activityi

Formamide = cyanide + H2O.UniRule annotation2 Publications

Kineticsi

  1. KM=109 mM for cyanide1 Publication
  2. KM=14.7 mM for fumaronitrile1 Publication
  3. KM=3.7 mM for 2-cyanopyridine1 Publication
  1. Vmax=6.8 mmol/min/mg enzyme with cyanide as substrate1 Publication
  2. Vmax=18.8 mmol/min/mg enzyme with fumaronitrile as substrate1 Publication
  3. Vmax=10.3 mmol/min/mg enzyme with 2-cyanopyridine as substrate1 Publication

pH dependencei

Optimum pH is 8-9. Active from pH 5.5 to pH 10.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei48Proton acceptorUniRule annotation1
Active sitei130UniRule annotation1
Active sitei165NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase

Enzyme and pathway databases

BRENDAi3.5.5.1 518
3.5.5.5 518

Names & Taxonomyi

Protein namesi
Recommended name:
Cyanide hydratase1 PublicationUniRule annotation (EC:4.2.1.66UniRule annotation1 Publication)
Short name:
CHTUniRule annotation
Alternative name(s):
Cyanide-degrading nitrilaseUniRule annotation
Formamide hydrolyaseUniRule annotation
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004321821 – 356Cyanide hydrataseAdd BLAST356

Expressioni

Inductioni

By cyanide.UniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliA9QXE0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 287CN hydrolasePROSITE-ProRule annotationAdd BLAST280

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0805 Eukaryota
COG0388 LUCA

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
IPR037544 CN_hydrolase
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

Sequencei

Sequence statusi: Complete.

A9QXE0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPVLKKYKA AAVNAEPGWF NLEESVRRTI HWIDEAGKAG CKFIAFPELW
60 70 80 90 100
IPGYPYWMWK VNYQESLPLL KKYRENSLPS DSDEMRRIRN AARANKIYVS
110 120 130 140 150
LGYSEVDLAS LYTTQVMISP SGDILNHRRK IRATHVERLV FGDGTGDTTE
160 170 180 190 200
SVIQTDIGRV GHLNCWENMN PFMKAYAASL GEQVHVAAWP LYPGKETLKY
210 220 230 240 250
PDPFTNVAEA NADLVTPAYA IETGTYTLAP WQTITAEGIK LNTPPGKDLE
260 270 280 290 300
DPHIYNGHGR IFGPDGQNLV PHPDKDFEGL LFVDIDLDEC HLSKSLADFG
310 320 330 340 350
GHYMRPDLIR LLVDTNRKDL VVREDRVNGG VEYTRTVDRV GLSTPLDIAN

TVDSEN
Length:356
Mass (Da):40,022
Last modified:February 5, 2008 - v1
Checksum:i0F0EBCBAD80706B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU282000 mRNA Translation: ABX75546.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU282000 mRNA Translation: ABX75546.1

3D structure databases

ProteinModelPortaliA9QXE0
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0805 Eukaryota
COG0388 LUCA

Enzyme and pathway databases

BRENDAi3.5.5.1 518
3.5.5.5 518

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
IPR037544 CN_hydrolase
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
ProtoNetiSearch...

Entry informationi

Entry nameiCHT_ASPNG
AccessioniPrimary (citable) accession number: A9QXE0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: February 5, 2008
Last modified: October 10, 2018
This is version 31 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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