Skip Header

Contribute Send feedback
Read comments (?) or add your own

P52708 (HNLS_SORBI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-(S)-hydroxymandelonitrile lyase
Short name=HNL
Short name=Hydroxynitrile lyase
EC=4.1.2.11

Cleaved into the following 2 chains:

  1. P-(S)-hydroxymandelonitrile lyase chain A
  2. P-(S)-hydroxymandelonitrile lyase chain B
OrganismSorghum bicolor (Sorghum) (Sorghum vulgare)
Taxonomic identifier4558 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Sorghum

Protein attributes

Sequence length510 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. Is involved in the catabolism of the cyanogenic glycoside dhurrin. Ref.1

Catalytic activity

(S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde.

Subunit structure

Heterotetramer of two A and two B chains. The A and B chains are linked by a disulfide bond.

Tissue specificity

Primary leaves of seedlings.

Post-translational modification

The N-terminus of chain A is blocked.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentvacuole

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionhydroxymandelonitrile lyase activity

Inferred from electronic annotation. Source: EC

serine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 338304P-(S)-hydroxymandelonitrile lyase chain A
PRO_0000004341
Chain339 – 510172P-(S)-hydroxymandelonitrile lyase chain B
PRO_0000004342

Sites

Active site2131
Active site4141
Active site4691

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Ref.1
Glycosylation3651N-linked (GlcNAc...) Potential
Disulfide bond121 ↔ 377Interchain (between A and B chains)
Disulfide bond277 ↔ 289
Disulfide bond313 ↔ 344Interchain (between A and B chains)

Experimental info

Sequence conflict2891C → E AA sequence Ref.3
Sequence conflict3001Q → E AA sequence Ref.3
Sequence conflict3391P → S AA sequence Ref.3
Sequence conflict3421D → E AA sequence Ref.3
Sequence conflict3441C → V AA sequence Ref.3
Sequence conflict357 – 3582EV → PL AA sequence Ref.3

Secondary structure

1 .......................................... 510
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52708 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 5BAD268ADFA42A8C

FASTA51056,319
        10         20         30         40         50         60 
MAVFISSSGS PGRATATTTT TTTLLLAVLA AAAAAGLLLA PVAARGSPPE HDKQLQLQQQ 

        70         80         90        100        110        120 
EDDRIPGLPG QPNGVAFGMY GGYVTIDDNN GRALYYWFQE ADTADPAAAP LVLWLNGGPG 

       130        140        150        160        170        180 
CSSIGLGAMQ ELGPFRVHTN GESLLLNEYA WNKAANILFA ESPAGVVFSY SNTSSDLSMG 

       190        200        210        220        230        240 
DDKMAQDTYT FLVKWFERFP HYNYREFYIA GESGHFIPQL SQVVYRNRNN SPFINFQGLL 

       250        260        270        280        290        300 
VSSGLTNDHE DMIGMFELWW HHGLISDETR DSGLKVCPGT SFMHPTPECT EVWNKALAEQ 

       310        320        330        340        350        360 
GNINPYTIYT PTCDREPSPY QRRFWAPHGR AAPPPLMLPP YDPCAVFNSI NYLNLPEVQT 

       370        380        390        400        410        420 
ALHANVSGIV EYPWTVCSNT IFDQWGQAAD DLLPVYRELI QAGLRVWVYS GDTDSVVPVS 

       430        440        450        460        470        480 
STRRSLAALE LPVKTSWYPW YMAPTEREVG GWSVQYEGLT YVSPSGAGHL VPVHRPAQAF 

       490        500        510 
LLFKQFLKGE PMPAEEKNDI LLPSEKAPFY

« Hide

References

[1]"Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme."
Lauble H., Miehlich B., Forster S., Wajant H., Effenberger F.
Biochemistry 41:12043-12050(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 56-325 IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-172.
[2]"Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases."
Wajant H., Mundry K.-W., Pfizenmaier K.
Plant Mol. Biol. 26:735-746(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-510, PARTIAL PROTEIN SEQUENCE.
Strain: cv. Sordan 79.
Tissue: Seedling.
[3]"Purification and protein characterisation of hydroxynitrile lyases from sorghum and almond."
Jansen J., Woker J., Kula M.-R.
Biotechnol. Appl. Biochem. 15:90-99(1992)
Cited for: PROTEIN SEQUENCE OF 185-220; 285-311 AND 339-358.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ421152 mRNA. Translation: CAD12888.1.
X84057 mRNA. Translation: CAA58876.1.
PIRS53311.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GXSX-ray2.30A/C56-325[»]
B/D338-495[»]
ProteinModelPortalP52708.
SMRP52708. Positions 59-325, 338-495.
ModBaseSearch...

Protein-protein interaction databases

STRING4558.Sb04g036350.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP52708.

Phylogenomic databases

eggNOGCOG2939.
HOGENOMHOG000198295.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14084.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52708.

Entry information

Entry nameHNLS_SORBI
AccessionPrimary (citable) accession number: P52708
Secondary accession number(s): Q8W4X3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 28, 2009
Last modified: April 3, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents