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Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi16 – 19Combined sources4
Helixi22 – 28Combined sources7
Beta strandi32 – 36Combined sources5
Helixi48 – 50Combined sources3
Helixi54 – 57Combined sources4
Helixi59 – 66Combined sources8
Beta strandi74 – 80Combined sources7
Helixi82 – 93Combined sources12
Helixi94 – 96Combined sources3
Beta strandi97 – 105Combined sources9
Beta strandi110 – 112Combined sources3
Helixi116 – 124Combined sources9
Beta strandi132 – 138Combined sources7
Beta strandi141 – 147Combined sources7
Helixi150 – 156Combined sources7
Helixi163 – 172Combined sources10
Helixi180 – 185Combined sources6
Turni191 – 193Combined sources3
Helixi194 – 196Combined sources3
Beta strandi199 – 203Combined sources5
Beta strandi208 – 210Combined sources3
Helixi212 – 221Combined sources10
Beta strandi225 – 229Combined sources5
Helixi237 – 240Combined sources4
Helixi242 – 255Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QJ4X-ray1.10A1-257[»]
1SC9X-ray1.80A1-257[»]
1SCIX-ray2.18A1-257[»]
1SCKX-ray1.70A1-257[»]
1SCQX-ray2.90A1-257[»]
1YASX-ray1.90A1-257[»]
1YB6X-ray1.54A2-257[»]
1YB7X-ray1.76A2-257[»]
2G4LX-ray1.84A1-257[»]
2YASX-ray1.72A1-257[»]
3C6XX-ray1.05A1-257[»]
3C6YX-ray1.25A1-257[»]
3C6ZX-ray1.05A1-257[»]
3C70X-ray1.05A1-257[»]
3YASX-ray1.85A1-257[»]
4YASX-ray2.00A1-257[»]
5YASX-ray2.20A1-257[»]
6YASX-ray2.20A1-257[»]
7YASX-ray1.75A1-257[»]
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.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QJ4X-ray1.10A1-257[»]
1SC9X-ray1.80A1-257[»]
1SCIX-ray2.18A1-257[»]
1SCKX-ray1.70A1-257[»]
1SCQX-ray2.90A1-257[»]
1YASX-ray1.90A1-257[»]
1YB6X-ray1.54A2-257[»]
1YB7X-ray1.76A2-257[»]
2G4LX-ray1.84A1-257[»]
2YASX-ray1.72A1-257[»]
3C6XX-ray1.05A1-257[»]
3C6YX-ray1.25A1-257[»]
3C6ZX-ray1.05A1-257[»]
3C70X-ray1.05A1-257[»]
3YASX-ray1.85A1-257[»]
4YASX-ray2.00A1-257[»]
5YASX-ray2.20A1-257[»]
6YASX-ray2.20A1-257[»]
7YASX-ray1.75A1-257[»]
ProteinModelPortaliP52704.
SMRiP52704.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERihevbr-hnl. Hydroxynitrile_lyase.

Proteomic databases

PRIDEiP52704.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC49184.

Phylogenomic databases

KOiK13033.

Enzyme and pathway databases

BRENDAi4.1.2.47. 2665.

Miscellaneous databases

EvolutionaryTraceiP52704.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHNL_HEVBR
AccessioniPrimary (citable) accession number: P52704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.