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Protein

Hevamine-A

Gene
N/A
Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei153Proton donor1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei1531. Hev b 14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000001195227 – 299Hevamine-AAdd BLAST273
PropeptideiPRO_0000011953300 – 311Removed in mature formAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 93
Disulfide bondi76 ↔ 83
Disulfide bondi185 ↔ 214

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP23472.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 35Combined sources8
Helixi37 – 39Combined sources3
Helixi42 – 47Combined sources6
Beta strandi52 – 61Combined sources10
Beta strandi66 – 69Combined sources4
Helixi73 – 75Combined sources3
Helixi79 – 81Combined sources3
Turni82 – 85Combined sources4
Helixi86 – 95Combined sources10
Beta strandi99 – 105Combined sources7
Helixi116 – 129Combined sources14
Beta strandi131 – 133Combined sources3
Beta strandi146 – 151Combined sources6
Helixi160 – 169Combined sources10
Helixi170 – 173Combined sources4
Beta strandi178 – 181Combined sources4
Beta strandi184 – 188Combined sources5
Turni190 – 192Combined sources3
Helixi193 – 197Combined sources5
Beta strandi202 – 207Combined sources6
Helixi212 – 214Combined sources3
Helixi222 – 234Combined sources13
Beta strandi238 – 247Combined sources10
Helixi248 – 250Combined sources3
Beta strandi251 – 253Combined sources3
Helixi258 – 263Combined sources6
Helixi266 – 269Combined sources4
Beta strandi275 – 281Combined sources7
Helixi283 – 289Combined sources7
Helixi291 – 295Combined sources5
Helixi296 – 298Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23472.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18_cat.
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)DescriptionActionsGraphical viewLength
Natural varianti296L → R in hevamine-B. 1
Natural varianti306E → K in hevamine-B. 1

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.
PIRiT10761.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1531. Hev b 14.
CAZyiGH18. Glycoside Hydrolase Family 18.

Proteomic databases

PRIDEiP23472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23472.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18_cat.
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]
ProtoNetiSearch...

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 2, 2016
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.