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P31757 (ALLN_ALLCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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 (Onion)
Taxonomic identifier4679 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Sequence caution

The sequence CAA78267.1 differs from that shown. Reason: Erroneous initiation.

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 – 2525 Potential
Propeptide26 – 349
PRO_0000020683
Chain35 – 479445Alliin lyase
PRO_0000020684

Regions

Domain47 – 9347EGF-like; atypical

Sites

Binding site1281Chloride By similarity
Binding site1321Chloride By similarity
Binding site1341Chloride By similarity

Amino acid modifications

Modified residue2851N6-(pyridoxal phosphate)lysine By similarity
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 73 By similarity
Disulfide bond75 ↔ 84 By similarity
Disulfide bond78 ↔ 91 By similarity
Disulfide bond402 ↔ 410 By similarity

Experimental info

Sequence conflict371S → T AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31757 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 2641AB82B8990230

FASTA47954,839
        10         20         30         40         50         60 
MESYDKVGSN KVPCLLILTC IIMSSFVNNN IVQAKVSWSL KAAEEAEAVA NINCSGHGRA 

        70         80         90        100        110        120 
FLDGILSDGS PKCECNTCYT GADCSEKITG CSADVASGDG LFLEEYWQQH KENSAVLVSG 

       130        140        150        160        170        180 
WHRMSYFFNP VSNFISFELE KTIKELHEIV GNAAAKDRYI VFGVGVTQLI HGLVISLSPN 

       190        200        210        220        230        240 
MTATPCAPQS KVVAHAPYYP VFREQTKYFD KKGYEWKGNA ADYVNTSTPE QFIEMVTSPN 

       250        260        270        280        290        300 
NPEGLLRHEV IKGCKSIYYM VYYWPHYTPI KYKADEDIML FTMSKYTGHS GSRFGWALIK 

       310        320        330        340        350        360 
DETVYNKLLN YMTKNTEGTS RETQLRSLKI LKEVIAMVKT QNGTMRDLNT FGFQKLRERW 

       370        380        390        400        410        420 
VNITALLDKS DRFSYQKLPQ SEYCNYFRRM RPPSPSYAWV KCEWEEDKDC YQTFQNGRIN 

       430        440        450        460        470 
TQSGEGFEAG SRYVRLSLIK TKDDFDQLMY YLKIMVEAKR KTPLIKQLSN DQISRRPFI 

« 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], PROTEIN SEQUENCE OF 35-54.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12621 mRNA. Translation: CAA78267.1. Different initiation.
PIRS29301.

3D structure databases

ProteinModelPortalP31757.
SMRP31757. Positions 35-461.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome842. All c Alliin lyase.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_ALLCE
AccessionPrimary (citable) accession number: P31757
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 79 of the entry and version 2 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