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P31756 (ALLN_ALLCG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Alliin lyase

Short name=Alliinase
EC=4.4.1.4
Alternative name(s):
Cysteine sulphoxide lyase
OrganismAllium cepa var. aggregatum (Shallot) (Allium ascalonicum)
Taxonomic identifier28911 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Protein attributes

Sequence length447 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Subcellular location

Vacuole.

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
   LigandChloride
Pyridoxal phosphate
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
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

Propeptide‹1 – 2›2
PRO_0000020681
Chain3 – 447445Alliin lyase
PRO_0000020682

Regions

Domain15 – 6147EGF-like; atypical

Sites

Binding site961Chloride By similarity
Binding site1001Chloride By similarity
Binding site1021Chloride By similarity

Amino acid modifications

Modified residue2531N6-(pyridoxal phosphate)lysine By similarity
Glycosylation211N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Disulfide bond22 ↔ 41 By similarity
Disulfide bond43 ↔ 52 By similarity
Disulfide bond46 ↔ 59 By similarity
Disulfide bond370 ↔ 378 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P31756 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: C4B389C81CCD45E7

FASTA44751,261
        10         20         30         40         50         60 
QAKVTWSLKA AEEAEAVANI NCSGHGRAFL DGILSDGSPK CECNTCYTGA DCSQKITGCS 

        70         80         90        100        110        120 
ADVASGDGLF LEEYWQQHKE NSAVLVSGWH RTSYFFNPVS NFISFELEKT IKELHEIVGN 

       130        140        150        160        170        180 
AAAKDRYIVF GVGVTQLIHG LVISLSPNMT ATPCAPQSKV VAHAPYYPVF REQTKYFDKK 

       190        200        210        220        230        240 
GYEWKGNAAD YVNTSTPEQF IEMVTSPNNP EGLLRHEVIK GCKSIYDMVY YWPHYTPIKY 

       250        260        270        280        290        300 
KADEDIMLFT MSKYTGHSGS RFGWALIKDE TVYNKLLNYM TKNTEGTSRE TQLRSLKILK 

       310        320        330        340        350        360 
EVTAMIKTQK GTMRDLNTFG FQKLRERWVN ITALLDKSDR FSYQKLPQSE YCNYFRRMRP 

       370        380        390        400        410        420 
PSPSYAWVKC EWEEDKDCYQ TFQNGRINTQ SGEGFEAGSR YVRLSLIKTK DDFDQLMYYL 

       430        440 
KIMVEAKRKT PLIKQLSNDQ ISRRPFI 

« Hide

References

[1]"Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species."
van Damme E.J.M., Smeets K., Torrekens S., van Leuven F., Peumans W.J.
Eur. J. Biochem. 209:751-757(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Shoot.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12620 mRNA. Translation: CAA78266.1.
PIRS29300.

3D structure databases

ProteinModelPortalP31756.
SMRP31756. Positions 3-429.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1254. All a Alliin lyase.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13494.

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 nameALLN_ALLCG
AccessionPrimary (citable) accession number: P31756
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 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