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P52705 (HNL_MANES) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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
OrganismManihot esculenta (Cassava) (Jatropha manihot)
Taxonomic identifier3983 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeManihoteaeManihot

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Homotrimer.

Sequence similarities

Belongs to the AB hydrolase superfamily. Hydroxynitrile lyase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 258257(S)-hydroxynitrile lyase
PRO_0000084018

Sites

Active site801 By similarity
Active site2081 By similarity
Active site2361 By similarity

Experimental info

Mutagenesis801S → A: Loss of activity. Ref.3

Secondary structure

.................................................. 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52705 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 98ABA050AC8AF1C5

FASTA25829,372
        10         20         30         40         50         60 
MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ INSFDEYSEP 

        70         80         90        100        110        120 
LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG VFHNSLLPDT VHSPSYTVEK 

       130        140        150        160        170        180 
LLESFPDWRD TEYFTFTNIT GETITTMKLG FVLLRENLFT KCTDGEYELA KMVMRKGSLF 

       190        200        210        220        230        240 
QNVLAQRPKF TEKGYGSIKK VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL 

       250 
TKTEEVAHIL QEVADAYA 

« Hide

References

[1]"Purification, characterization, and cloning of alpha-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)."
Hughes J., Carvalho F.J.P.D.C., Hughes M.A.
Arch. Biochem. Biophys. 311:496-502(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-37 AND 169-192.
Tissue: Cotyledon.
[2]"Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis."
Lauble H., Foerster S., Miehlich B., Wajant H., Effenberger F.
Acta Crystallogr. D 57:194-200(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]"Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin."
Lauble H., Miehlich B., Foerster S., Wajant H., Effenberger F.
Protein Sci. 10:1015-1022(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF SER-80.
[4]"Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta."
Lauble H., Miehlich B., Foerster S., Kobler C., Wajant H., Effenberger F.
Protein Sci. 11:65-71(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29091 mRNA. Translation: CAA82334.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DWOX-ray2.20A/B1-258[»]
1DWPX-ray2.20A/B1-258[»]
1DWQX-ray2.20A/B1-258[»]
1E89X-ray2.10A/B1-258[»]
1E8DX-ray2.20A/B1-258[»]
1EB8X-ray2.10A/B1-258[»]
1EB9X-ray2.10A/B1-258[»]
3RKSX-ray2.50A/B/C/D1-258[»]
3RKTX-ray2.91A/B/C/D/E/F/G/H1-258[»]
ProteinModelPortalP52705.
SMRP52705. Positions 1-258.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-6902.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52705.

Entry information

Entry nameHNL_MANES
AccessionPrimary (citable) accession number: P52705
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 72 of the entry and version 3 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