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P31756

- ALLN_ALLCG

UniProt

P31756 - ALLN_ALLCG

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Protein

Alliin lyase

Gene
N/A
Organism
Allium cepa var. aggregatum (Shallot) (Allium ascalonicum)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961Chloride By similarity
Binding sitei100 – 1001Chloride By similarity
Binding sitei102 – 1021Chloride By similarity

GO - Molecular functioni

  1. alliin lyase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Chloride, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13494.

Names & Taxonomyi

Protein namesi
Recommended name:
Alliin lyase (EC:4.4.1.4)
Short name:
Alliinase
Alternative name(s):
Cysteine sulphoxide lyase
OrganismiAllium cepa var. aggregatum (Shallot) (Allium ascalonicum)
Taxonomic identifieri28911 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Subcellular locationi

GO - Cellular componenti

  1. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei1254. All a Alliin lyase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei‹1 – 2›2PRO_0000020681
Chaini3 – 447445Alliin lyasePRO_0000020682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi21 – 211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi22 ↔ 41 By similarity
Disulfide bondi43 ↔ 52 By similarity
Disulfide bondi46 ↔ 59 By similarity
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi193 – 1931N-linked (GlcNAc...) Reviewed prediction
Modified residuei253 – 2531N6-(pyridoxal phosphate)lysine By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi370 ↔ 378 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP31756.
SMRiP31756. Positions 3-429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 6147EGF-like; atypicalAdd
BLAST

Domaini

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 similaritiesi

Belongs to the alliinase family.
Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31756-1 [UniParc]FASTAAdd to Basket

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QAKVTWSLKA AEEAEAVANI NCSGHGRAFL DGILSDGSPK CECNTCYTGA    50
DCSQKITGCS ADVASGDGLF LEEYWQQHKE NSAVLVSGWH RTSYFFNPVS 100
NFISFELEKT IKELHEIVGN AAAKDRYIVF GVGVTQLIHG LVISLSPNMT 150
ATPCAPQSKV VAHAPYYPVF REQTKYFDKK GYEWKGNAAD YVNTSTPEQF 200
IEMVTSPNNP EGLLRHEVIK GCKSIYDMVY YWPHYTPIKY KADEDIMLFT 250
MSKYTGHSGS RFGWALIKDE TVYNKLLNYM TKNTEGTSRE TQLRSLKILK 300
EVTAMIKTQK GTMRDLNTFG FQKLRERWVN ITALLDKSDR FSYQKLPQSE 350
YCNYFRRMRP PSPSYAWVKC EWEEDKDCYQ TFQNGRINTQ SGEGFEAGSR 400
YVRLSLIKTK DDFDQLMYYL KIMVEAKRKT PLIKQLSNDQ ISRRPFI 447
Length:447
Mass (Da):51,261
Last modified:July 1, 1993 - v1
Checksum:iC4B389C81CCD45E7
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12620 mRNA. Translation: CAA78266.1.
PIRiS29300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12620 mRNA. Translation: CAA78266.1 .
PIRi S29300.

3D structure databases

ProteinModelPortali P31756.
SMRi P31756. Positions 3-429.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 1254. All a Alliin lyase.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13494.

Family and domain databases

Gene3Di 2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00022. EGF_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiALLN_ALLCG
AccessioniPrimary (citable) accession number: P31756
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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