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Q41233 (ALLN2_ALLSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alliin lyase 2

Short name=Alliinase-2
EC=4.4.1.4
Alternative name(s):
Cysteine sulphoxide lyase 2
OrganismAllium sativum (Garlic)
Taxonomic identifier4682 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.

Catalytic activity

An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Vacuole.

Tissue specificity

High expression in bulbs, lower expression in leaves, and no expression in roots.

Domain

The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor By similarity.

Sequence similarities

Belongs to the alliinase family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentVacuole
   DomainEGF-like domain
Signal
   LigandChloride
Pyridoxal phosphate
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalliin lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Propeptide16 – 2510 By similarity
PRO_0000020679
Chain26 – 473448Alliin lyase 2
PRO_0000020680

Regions

Domain38 – 8447EGF-like; atypical

Sites

Binding site1191Chloride By similarity
Binding site1231Chloride By similarity
Binding site1251Chloride By similarity

Amino acid modifications

Modified residue2761N6-(pyridoxal phosphate)lysine By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 64 By similarity
Disulfide bond66 ↔ 75 By similarity
Disulfide bond69 ↔ 82 By similarity
Disulfide bond393 ↔ 401 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q41233 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 19F08669BA95A047

FASTA47354,183
        10         20         30         40         50         60 
MICLVILTCI IMSNSFVNNN NMVQAKMTWT MKAAEEAEAV ANINCSEHGR AFLDGIISEG 

        70         80         90        100        110        120 
SPKCECNTCY TGPDCSEKIQ GCSADVASGD GLFLEEYWKQ HKEASAVLVS PWHRMSYFFN 

       130        140        150        160        170        180 
PVSNFISFEL EKTIKELHEV VGNAAAKDRY IVFGVGVTQL IHGLVISLSP NMTATPDAPE 

       190        200        210        220        230        240 
SKVVAHAPFY PVFREQTKYF DKKGYVWAGN AANYVNVSNP EQYIEMVTSP NNPEGLLRHA 

       250        260        270        280        290        300 
VIKGCKSIYD MVYYWPHYTP IKYKADEDIL LFTMSKFTGH SGSRFGWALI KDESVYNNLL 

       310        320        330        340        350        360 
NYMTKNTEGT PRETQLRSLK VLKEIVAMVK TQKGTMRDLN TFGFKKLRER WVNITALLDQ 

       370        380        390        400        410        420 
SDRFSYQELP QSEYCNYFRR MRPPSPSYAW VNCEWEEDKD CYQTFQNGRI NTQSGVGFEA 

       430        440        450        460        470 
SSRYVRLSLI KTQDDFDQLM YYLKDMVKAK RKTPLIKQLF TDETETASRR PFI 

« Hide

References

[1]"Alliin lyase (Alliinase) from garlic (Allium sativum). Biochemical characterization and cDNA cloning."
Rabinkov A., Zhu X.Z., Grafi G., Galili G., Mirelman D.
Appl. Biochem. Biotechnol. 48:149-171(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Tissue: Bulb.

Web resources

Protein Spotlight

What's that smell? - Issue 39 of October 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S73324 mRNA. Translation: AAB32477.1.

3D structure databases

ProteinModelPortalQ41233.
SMRQ41233. Positions 26-452.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome843. All s Alliin lyase.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13491.

Family and domain databases

Gene3D2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALLN2_ALLSA
AccessionPrimary (citable) accession number: Q41233
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 79 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries