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Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.

Catalytic activityi

An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone.
An aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei801
Active sitei2071
Active sitei2351

GO - Molecular functioni

Keywordsi

Molecular functionLyase

Enzyme and pathway databases

BRENDAi4.1.2.47 2665

Protein family/group databases

ESTHERihevbr-hnl Hydroxynitrile_lyase

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-hydroxynitrile lyase (EC:4.1.2.47)
Alternative name(s):
(S)-acetone-cyanohydrin lyase
Oxynitrilase
Gene namesi
Name:HNL
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80S → A: Loss of activity. 1 Publication1
Mutagenesisi81C → S: Loss of activity. 1 Publication1
Mutagenesisi235H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000840171 – 257(S)-hydroxynitrile lyaseAdd BLAST257

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP52704

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP52704
SMRiP52704
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52704

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 241AB hydrolase-1Sequence analysisAdd BLAST237

Sequence similaritiesi

Phylogenomic databases

KOiK13033

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit

Sequencei

Sequence statusi: Complete.

P52704-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE
60 70 80 90 100
IGSFDEYSEP LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA
110 120 130 140 150
VFHNSVLPDT EHCPSYVVDK LMEVFPDWKD TTYFTYTKDG KEITGLKLGF
160 170 180 190 200
TLLRENLYTL CGPEEYELAK MLTRKGSLFQ NILAKRPFFT KEGYGSIKKI
210 220 230 240 250
YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT KTKEIAEILQ

EVADTYN
Length:257
Mass (Da):29,228
Last modified:October 1, 1996 - v1
Checksum:iEF4AE88717279CEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40402 mRNA Translation: AAC49184.1
PIRiT10758

Genome annotation databases

KEGGiag:AAC49184

Similar proteinsi

Entry informationi

Entry nameiHNL_HEVBR
AccessioniPrimary (citable) accession number: P52704
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 15, 2017
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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