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P31757

- ALLN_ALLCE

UniProt

P31757 - ALLN_ALLCE

Protein

Alliin lyase

Gene
N/A
Organism
Allium cepa (Onion)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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 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

    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-SubCell

    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

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    MESYDKVGSN KVPCLLILTC IIMSSFVNNN IVQAKVSWSL KAAEEAEAVA    50
    NINCSGHGRA FLDGILSDGS PKCECNTCYT GADCSEKITG CSADVASGDG 100
    LFLEEYWQQH KENSAVLVSG WHRMSYFFNP VSNFISFELE KTIKELHEIV 150
    GNAAAKDRYI VFGVGVTQLI HGLVISLSPN MTATPCAPQS KVVAHAPYYP 200
    VFREQTKYFD KKGYEWKGNA ADYVNTSTPE QFIEMVTSPN NPEGLLRHEV 250
    IKGCKSIYYM VYYWPHYTPI KYKADEDIML FTMSKYTGHS GSRFGWALIK 300
    DETVYNKLLN YMTKNTEGTS RETQLRSLKI LKEVIAMVKT QNGTMRDLNT 350
    FGFQKLRERW VNITALLDKS DRFSYQKLPQ SEYCNYFRRM RPPSPSYAWV 400
    KCEWEEDKDC YQTFQNGRIN TQSGEGFEAG SRYVRLSLIK TKDDFDQLMY 450
    YLKIMVEAKR KTPLIKQLSN DQISRRPFI 479
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12621 mRNA. Translation: CAA78267.1. Different initiation.
    PIRiS29301.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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: October 1, 2014
    This is version 80 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