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P23472

- CHLY_HEVBR

UniProt

P23472 - CHLY_HEVBR

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 358Combined sources
Helixi37 – 393Combined sources
Helixi42 – 476Combined sources
Beta strandi52 – 6110Combined sources
Beta strandi66 – 694Combined sources
Helixi73 – 753Combined sources
Helixi79 – 813Combined sources
Turni82 – 854Combined sources
Helixi86 – 9510Combined sources
Beta strandi99 – 1057Combined sources
Helixi116 – 12914Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi146 – 1516Combined sources
Helixi160 – 16910Combined sources
Helixi170 – 1734Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1885Combined sources
Turni190 – 1923Combined sources
Helixi193 – 1975Combined sources
Beta strandi202 – 2076Combined sources
Helixi212 – 2143Combined sources
Helixi222 – 23413Combined sources
Beta strandi238 – 24710Combined sources
Helixi248 – 2503Combined sources
Beta strandi251 – 2533Combined sources
Helixi258 – 2636Combined sources
Helixi266 – 2694Combined sources
Beta strandi275 – 2817Combined sources
Helixi283 – 2897Combined sources
Helixi291 – 2955Combined sources
Helixi296 – 2983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK
60 70 80 90 100
YSYVNIAFLN KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV
110 120 130 140 150
MLSLGGGIGS YTLASQADAK NVADYLWNNF LGGKSSSRPL GDAVLDGIDF
160 170 180 190 200
DIEHGSTLYW DDLARYLSAY SKQGKKVYLT AAPQCPFPDR YLGTALNTGL
210 220 230 240 250
FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI FLGLPAAPEA
260 270 280 290 300
AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL
310
FLHSEECMTV L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 102 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