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P31757

- ALLN_ALLCE

UniProt

P31757 - ALLN_ALLCE

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Protein

Alliin lyase

Gene
N/A
Organism
Allium cepa (Onion)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281ChlorideBy similarity
Binding sitei132 – 1321ChlorideBy similarity
Binding sitei134 – 1341ChlorideBy 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

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

  1. vacuole Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 3491 PublicationPRO_0000020683
Chaini35 – 479445Alliin lyasePRO_0000020684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi54 ↔ 73By similarity
Disulfide bondi75 ↔ 84By similarity
Disulfide bondi78 ↔ 91By similarity
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence Analysis
Modified residuei285 – 2851N6-(pyridoxal phosphate)lysineBy similarity
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi402 ↔ 410By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP31757.
SMRiP31757. Positions 35-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9347EGF-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).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 CAA78267.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371S → T AA sequence (PubMed:1385120)Curated

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.
PIRi S29301.

3D structure databases

ProteinModelPortali P31757.
SMRi P31757. Positions 35-461.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 842. All c Alliin lyase.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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], PROTEIN SEQUENCE OF 35-54.

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: November 26, 2014
This is version 82 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

External Data

Dasty 3