Reviewed, UniProtKB/Swiss-Prot P23472 (CHLY_HEVBR)

Names and origin

Protein names	Recommended name:     Hevamine-A Including the following 2 domains:     1- Recommended name:             Chitinase               EC=3.2.1.14     2- Recommended name:             Lysozyme               EC=3.2.1.17
Organism	Hevea brasiliensis (Para rubber tree)
Taxonomic identifier	3981 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Malpighiales › Euphorbiaceae › Crotonoideae › Micrandreae › Hevea

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Vacuole
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro chitinase activity Inferred from electronic annotation. Source: EC lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.3

Chain

27 – 299

273

Hevamine-A

PRO_0000011952

Propeptide

300 – 311

12

Removed in mature form

PRO_0000011953

Sites

Active site

153

1

Proton donor

Amino acid modifications

Disulfide bond

46 ↔ 93

Disulfide bond

76 ↔ 83

Disulfide bond

185 ↔ 214

Natural variations

Natural variant

296

1

L → R in hevamine-B.

Natural variant

306

1

E → K in hevamine-B.

Secondary structure

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311

Helix Strand Turn

Details...

Beta strand

28 – 35

8

Helix

37 – 39

3

Helix

42 – 47

6

Beta strand

51 – 63

13

Beta strand

66 – 70

5

Helix

79 – 85

7

Helix

86 – 95

10

Beta strand

99 – 105

7

Helix

116 – 130

15

Beta strand

131 – 133

3

Beta strand

146 – 151

6

Helix

160 – 170

11

Beta strand

173 – 175

3

Beta strand

178 – 181

4

Beta strand

184 – 188

5

Turn

190 – 192

3

Helix

193 – 196

4

Beta strand

202 – 207

6

Helix

212 – 214

3

Helix

222 – 234

13

Beta strand

238 – 247

10

Helix

248 – 250

3

Beta strand

251 – 253

3

Helix

258 – 264

7

Helix

266 – 269

4

Beta strand

275 – 281

7

Helix

283 – 289

7

Helix

291 – 295

5

Helix

296 – 298

3

Sequences

	Sequence		Length	Mass (Da)
	P23472-1 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: 2CEED8658A28C908	FASTA	311	33,718
	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

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: 1879417] [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: 7704528] [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: 7495789] [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: 8831791] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ007701 Genomic DNA. Translation: CAA07608.1.
DQ873889 mRNA. Translation: ABI32402.2.
AJ010397 mRNA. Translation: CAA09110.1.

PIR

T10761.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA

3.2.1.14. 2218.
3.2.1.17. 2218.

Family and domain databases

InterPro

IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHLY_HEVBR

Accession

Primary (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:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)