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P52704 (HNL_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(S)-hydroxynitrile lyase

EC=4.1.2.47
Alternative name(s):
(S)-acetone-cyanohydrin lyase
Oxynitrilase
Gene names
Name:HNL
OrganismHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifier3981 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

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

Subunit structure

Homodimer.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the AB hydrolase superfamily. Hydroxynitrile lyase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257(S)-hydroxynitrile lyase
PRO_0000084017

Sites

Active site801
Active site2071
Active site2351

Experimental info

Mutagenesis801S → A: Loss of activity. Ref.2
Mutagenesis811C → S: Loss of activity. Ref.1
Mutagenesis2351H → A: Loss of activity. Ref.2

Secondary structure

.................................................. 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52704 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EF4AE88717279CEB

FASTA25729,228
        10         20         30         40         50         60 
MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE IGSFDEYSEP 

        70         80         90        100        110        120 
LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA VFHNSVLPDT EHCPSYVVDK 

       130        140        150        160        170        180 
LMEVFPDWKD TTYFTYTKDG KEITGLKLGF TLLRENLYTL CGPEEYELAK MLTRKGSLFQ 

       190        200        210        220        230        240 
NILAKRPFFT KEGYGSIKKI YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT 

       250 
KTKEIAEILQ EVADTYN 

« Hide

References

[1]"Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue."
Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., Schwab H.
J. Biol. Chem. 271:5884-5891(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 121-126; 176-181; 200-204 AND 244-253, MUTAGENESIS OF CYS-81.
Tissue: Leaf.
[2]"Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
Wagner U.G., Hasslacher M., Griengl H., Schwab H., Kratky C.
Structure 4:811-822(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF SER-80 AND HIS-235.
[3]"Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
Gruber K., Gugganig M., Wagner U.G., Kratky C.
Biol. Chem. 380:993-1000(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
[4]"Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis."
Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C.
Protein Sci. 8:1990-2000(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40402 mRNA. Translation: AAC49184.1.
PIRT10758.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP52704.
SMRP52704. Positions 2-257.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP52704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP52704.

Entry information

Entry nameHNL_HEVBR
AccessionPrimary (citable) accession number: P52704
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references