Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alliin lyase

Gene
N/A
Organism
Allium cepa (Onion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei128ChlorideBy similarity1
Binding sitei132ChlorideBy similarity1
Binding sitei134ChlorideBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Chloride, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Alliin lyase (EC:4.4.1.4)
Short name:
Alliinase
Alternative name(s):
Cysteine sulphoxide lyase
OrganismiAllium cepa (Onion)
Taxonomic identifieri4679 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei842. All c Alliin lyase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
PropeptideiPRO_000002068326 – 341 Publication9
ChainiPRO_000002068435 – 479Alliin lyaseAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi54 ↔ 73By similarity
Disulfide bondi75 ↔ 84By similarity
Disulfide bondi78 ↔ 91By similarity
Glycosylationi180N-linked (GlcNAc...)Sequence analysis1
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Modified residuei285N6-(pyridoxal phosphate)lysineBy similarity1
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi402 ↔ 410By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP31757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 93EGF-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, Signal

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: Complete.

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

P31757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESYDKVGSN KVPCLLILTC IIMSSFVNNN IVQAKVSWSL KAAEEAEAVA
60 70 80 90 100
NINCSGHGRA FLDGILSDGS PKCECNTCYT GADCSEKITG CSADVASGDG
110 120 130 140 150
LFLEEYWQQH KENSAVLVSG WHRMSYFFNP VSNFISFELE KTIKELHEIV
160 170 180 190 200
GNAAAKDRYI VFGVGVTQLI HGLVISLSPN MTATPCAPQS KVVAHAPYYP
210 220 230 240 250
VFREQTKYFD KKGYEWKGNA ADYVNTSTPE QFIEMVTSPN NPEGLLRHEV
260 270 280 290 300
IKGCKSIYYM VYYWPHYTPI KYKADEDIML FTMSKYTGHS GSRFGWALIK
310 320 330 340 350
DETVYNKLLN YMTKNTEGTS RETQLRSLKI LKEVIAMVKT QNGTMRDLNT
360 370 380 390 400
FGFQKLRERW VNITALLDKS DRFSYQKLPQ SEYCNYFRRM RPPSPSYAWV
410 420 430 440 450
KCEWEEDKDC YQTFQNGRIN TQSGEGFEAG SRYVRLSLIK TKDDFDQLMY
460 470
YLKIMVEAKR KTPLIKQLSN DQISRRPFI
Length:479
Mass (Da):54,839
Last modified:June 1, 1994 - v2
Checksum:i2641AB82B8990230
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37S → T AA sequence (PubMed:1385120).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12621 mRNA. Translation: CAA78267.1. Different initiation.
PIRiS29301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12621 mRNA. Translation: CAA78267.1. Different initiation.
PIRiS29301.

3D structure databases

ProteinModelPortaliP31757.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei842. All c Alliin lyase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_ALLCE
AccessioniPrimary (citable) accession number: P31757
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 1, 1994
Last modified: October 5, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.