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P23472 (CHLY_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hevamine-A

Including the following 2 domains:

  1. Chitinase
    EC=3.2.1.14
  2. Lysozyme
    EC=3.2.1.17
OrganismHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifier3981 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subcellular location

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

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

lysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.3
Chain27 – 299273Hevamine-A
PRO_0000011952
Propeptide300 – 31112Removed in mature form
PRO_0000011953

Sites

Active site1531Proton donor

Amino acid modifications

Disulfide bond46 ↔ 93
Disulfide bond76 ↔ 83
Disulfide bond185 ↔ 214

Natural variations

Natural variant2961L → R in hevamine-B.
Natural variant3061E → K in hevamine-B.

Secondary structure

........................................................ 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23472 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 2CEED8658A28C908

FASTA31133,718
        10         20         30         40         50         60 
MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK YSYVNIAFLN 

        70         80         90        100        110        120 
KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV MLSLGGGIGS YTLASQADAK 

       130        140        150        160        170        180 
NVADYLWNNF LGGKSSSRPL GDAVLDGIDF DIEHGSTLYW DDLARYLSAY SKQGKKVYLT 

       190        200        210        220        230        240 
AAPQCPFPDR YLGTALNTGL FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI 

       250        260        270        280        290        300 
FLGLPAAPEA AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL 

       310 
FLHSEECMTV L 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007701 Genomic DNA. Translation: CAA07608.1.
DQ873889 mRNA. Translation: ABI32402.2.
AJ010397 mRNA. Translation: CAA09110.1.
PIRT10761.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP23472.
SMRP23472. Positions 27-299.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1531. Hev b 14.
CAZyGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23472.

Entry information

Entry nameCHLY_HEVBR
AccessionPrimary (citable) accession number: P23472
Secondary accession number(s): Q0GBZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 15, 2002
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries