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Protein

Alliin lyase

Gene
N/A
Organism
Allium cepa var. aggregatum (Shallot) (Allium ascalonicum)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96ChlorideBy similarity1
Binding sitei100ChlorideBy similarity1
Binding sitei102ChlorideBy similarity1

GO - Molecular functioni

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

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000020681‹1 – 2›2
ChainiPRO_00000206823 – 447Alliin lyaseAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi22 ↔ 41By similarity
Disulfide bondi43 ↔ 52By similarity
Disulfide bondi46 ↔ 59By similarity
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi193N-linked (GlcNAc...)Sequence analysis1
Modified residuei253N6-(pyridoxal phosphate)lysineBy similarity1
Glycosylationi330N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi370 ↔ 378By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP31756.
SMRiP31756.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 61EGF-like; atypicalAdd BLAST47

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).By similarity

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
QAKVTWSLKA AEEAEAVANI NCSGHGRAFL DGILSDGSPK CECNTCYTGA
60 70 80 90 100
DCSQKITGCS ADVASGDGLF LEEYWQQHKE NSAVLVSGWH RTSYFFNPVS
110 120 130 140 150
NFISFELEKT IKELHEIVGN AAAKDRYIVF GVGVTQLIHG LVISLSPNMT
160 170 180 190 200
ATPCAPQSKV VAHAPYYPVF REQTKYFDKK GYEWKGNAAD YVNTSTPEQF
210 220 230 240 250
IEMVTSPNNP EGLLRHEVIK GCKSIYDMVY YWPHYTPIKY KADEDIMLFT
260 270 280 290 300
MSKYTGHSGS RFGWALIKDE TVYNKLLNYM TKNTEGTSRE TQLRSLKILK
310 320 330 340 350
EVTAMIKTQK GTMRDLNTFG FQKLRERWVN ITALLDKSDR FSYQKLPQSE
360 370 380 390 400
YCNYFRRMRP PSPSYAWVKC EWEEDKDCYQ TFQNGRINTQ SGEGFEAGSR
410 420 430 440
YVRLSLIKTK DDFDQLMYYL KIMVEAKRKT PLIKQLSNDQ ISRRPFI
Length:447
Mass (Da):51,261
Last modified:July 1, 1993 - v1
Checksum:iC4B389C81CCD45E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12620 mRNA. Translation: CAA78266.1.
PIRiS29300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12620 mRNA. Translation: CAA78266.1.
PIRiS29300.

3D structure databases

ProteinModelPortaliP31756.
SMRiP31756.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1254. All a Alliin lyase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13494.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 84 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.