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P23472

- CHLY_HEVBR

UniProt

P23472 - CHLY_HEVBR

Protein

Hevamine-A

Gene
N/A
Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
    Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei153 – 1531Proton donor

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB-EC
    2. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB-KW
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hevamine-A
    Including the following 2 domains:
    Chitinase (EC:3.2.1.14)
    Lysozyme (EC:3.2.1.17)
    OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
    Taxonomic identifieri3981 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

    Subcellular locationi

    Vacuole
    Note: In the lutoids (vacuoles) from rubber latex.

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    Pathology & Biotechi

    Protein family/group databases

    Allergomei1531. Hev b 14.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 299273Hevamine-APRO_0000011952Add
    BLAST
    Propeptidei300 – 31112Removed in mature formPRO_0000011953Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 93
    Disulfide bondi76 ↔ 83
    Disulfide bondi185 ↔ 214

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 358
    Helixi37 – 393
    Helixi42 – 476
    Beta strandi52 – 6110
    Beta strandi66 – 694
    Helixi73 – 753
    Helixi79 – 813
    Turni82 – 854
    Helixi86 – 9510
    Beta strandi99 – 1057
    Helixi116 – 12914
    Beta strandi131 – 1333
    Beta strandi146 – 1516
    Helixi160 – 16910
    Helixi170 – 1734
    Beta strandi178 – 1814
    Beta strandi184 – 1885
    Turni190 – 1923
    Helixi193 – 1975
    Beta strandi202 – 2076
    Helixi212 – 2143
    Helixi222 – 23413
    Beta strandi238 – 24710
    Helixi248 – 2503
    Beta strandi251 – 2533
    Helixi258 – 2636
    Helixi266 – 2694
    Beta strandi275 – 2817
    Helixi283 – 2897
    Helixi291 – 2955
    Helixi296 – 2983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HVQX-ray2.20A27-299[»]
    1KQYX-ray1.92A27-299[»]
    1KQZX-ray1.92A27-299[»]
    1KR0X-ray1.92A27-299[»]
    1KR1X-ray2.00A27-299[»]
    1LLOX-ray1.85A27-299[»]
    2HVMX-ray1.80A27-299[»]
    ProteinModelPortaliP23472.
    SMRiP23472. Positions 27-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23472.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00704. Glyco_hydro_18. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS01095. CHITINASE_18. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23472-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK    50
    YSYVNIAFLN KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV 100
    MLSLGGGIGS YTLASQADAK NVADYLWNNF LGGKSSSRPL GDAVLDGIDF 150
    DIEHGSTLYW DDLARYLSAY SKQGKKVYLT AAPQCPFPDR YLGTALNTGL 200
    FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI FLGLPAAPEA 250
    AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL 300
    FLHSEECMTV L 311
    Length:311
    Mass (Da):33,718
    Last modified:May 15, 2002 - v2
    Checksum:i2CEED8658A28C908
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti296 – 2961L → R in hevamine-B.
    Natural varianti306 – 3061E → K in hevamine-B.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007701 Genomic DNA. Translation: CAA07608.1.
    DQ873889 mRNA. Translation: ABI32402.2.
    AJ010397 mRNA. Translation: CAA09110.1.
    PIRiT10761.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007701 Genomic DNA. Translation: CAA07608.1 .
    DQ873889 mRNA. Translation: ABI32402.2 .
    AJ010397 mRNA. Translation: CAA09110.1 .
    PIRi T10761.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HVQ X-ray 2.20 A 27-299 [» ]
    1KQY X-ray 1.92 A 27-299 [» ]
    1KQZ X-ray 1.92 A 27-299 [» ]
    1KR0 X-ray 1.92 A 27-299 [» ]
    1KR1 X-ray 2.00 A 27-299 [» ]
    1LLO X-ray 1.85 A 27-299 [» ]
    2HVM X-ray 1.80 A 27-299 [» ]
    ProteinModelPortali P23472.
    SMRi P23472. Positions 27-299.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 1531. Hev b 14.
    CAZyi GH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P23472.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001223. Glyco_hydro18cat.
    IPR001579. Glyco_hydro_18_chit_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00704. Glyco_hydro_18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS01095. CHITINASE_18. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Bokma E.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. RRIM.
      Tissue: Latex and Leaf.
    2. "Cloning and sequencing of chitinase gene in Hevea brasiliensis."
      Philip S., Abraham T., Joseph A., Zacharia C.A., Jacob C.K.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex."
      Jekel P.A., Hartmann J.B.H., Beintema J.J.
      Eur. J. Biochem. 200:123-130(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-299.
      Tissue: Latex.
    4. "Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor."
      van Scheltinga A.C.T., Kalk K.H., Beintema J.J., Dijkstra B.W.
      Structure 2:1181-1189(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    5. "Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis."
      van Scheltinga A.C.T., Armand S., Kalk K.H., Isogai A., Henrissat B., Dijkstra B.W.
      Biochemistry 34:15619-15623(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    6. "The 1.8-A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18."
      van Scheltinga A.C.T., Hennig M., Dijkstra B.W.
      J. Mol. Biol. 262:243-257(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiCHLY_HEVBR
    AccessioniPrimary (citable) accession number: P23472
    Secondary accession number(s): Q0GBZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two components of hevamine have been isolated: hevamine A (shown here), the most abundant, and hevamine B.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3