CHLY_HEVBR
ID CHLY_HEVBR Reviewed; 311 AA.
AC P23472; Q0GBZ6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Hevamine-A;
DE Includes:
DE RecName: Full=Chitinase;
DE EC=3.2.1.14;
DE Includes:
DE RecName: Full=Lysozyme;
DE EC=3.2.1.17;
DE Flags: Precursor;
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. RRIM; TISSUE=Latex, and Leaf;
RA Bokma E.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Philip S., Abraham T., Joseph A., Zacharia C.A., Jacob C.K.;
RT "Cloning and sequencing of chitinase gene in Hevea brasiliensis.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 27-299.
RC TISSUE=Latex;
RX PubMed=1879417; DOI=10.1111/j.1432-1033.1991.tb21057.x;
RA Jekel P.A., Hartmann J.B.H., Beintema J.J.;
RT "The primary structure of hevamine, an enzyme with lysozyme/chitinase
RT activity from Hevea brasiliensis latex.";
RL Eur. J. Biochem. 200:123-130(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7704528; DOI=10.1016/s0969-2126(94)00120-0;
RA van Scheltinga A.C.T., Kalk K.H., Beintema J.J., Dijkstra B.W.;
RT "Crystal structures of hevamine, a plant defence protein with chitinase and
RT lysozyme activity, and its complex with an inhibitor.";
RL Structure 2:1181-1189(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=7495789; DOI=10.1021/bi00048a003;
RA van Scheltinga A.C.T., Armand S., Kalk K.H., Isogai A., Henrissat B.,
RA Dijkstra B.W.;
RT "Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-
RT ray structure of a complex with allosamidin: evidence for substrate
RT assisted catalysis.";
RL Biochemistry 34:15619-15623(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=8831791; DOI=10.1006/jmbi.1996.0510;
RA van Scheltinga A.C.T., Hennig M., Dijkstra B.W.;
RT "The 1.8-A resolution structure of hevamine, a plant chitinase/lysozyme,
RT and analysis of the conserved sequence and structure motifs of glycosyl
RT hydrolase family 18.";
RL J. Mol. Biol. 262:243-257(1996).
CC -!- FUNCTION: Bifunctional enzyme with lysozyme / chitinase activity. May
CC have a role in plugging the latex vessel and cessation of latex flow.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17;
CC -!- SUBCELLULAR LOCATION: Vacuole. Note=In the lutoids (vacuoles) from
CC rubber latex.
CC -!- MISCELLANEOUS: Two components of hevamine have been isolated: hevamine
CC A (shown here), the most abundant, and hevamine B.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; AJ007701; CAA07608.1; -; Genomic_DNA.
DR EMBL; DQ873889; ABI32402.2; -; mRNA.
DR EMBL; AJ010397; CAA09110.1; -; mRNA.
DR PIR; T10761; T10761.
DR PDB; 1HVQ; X-ray; 2.20 A; A=27-299.
DR PDB; 1KQY; X-ray; 1.92 A; A=27-299.
DR PDB; 1KQZ; X-ray; 1.92 A; A=27-299.
DR PDB; 1KR0; X-ray; 1.92 A; A=27-299.
DR PDB; 1KR1; X-ray; 2.00 A; A=27-299.
DR PDB; 1LLO; X-ray; 1.85 A; A=27-299.
DR PDB; 2HVM; X-ray; 1.80 A; A=27-299.
DR PDBsum; 1HVQ; -.
DR PDBsum; 1KQY; -.
DR PDBsum; 1KQZ; -.
DR PDBsum; 1KR0; -.
DR PDBsum; 1KR1; -.
DR PDBsum; 1LLO; -.
DR PDBsum; 2HVM; -.
DR AlphaFoldDB; P23472; -.
DR SMR; P23472; -.
DR Allergome; 1531; Hev b 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EvolutionaryTrace; P23472; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Multifunctional enzyme; Polysaccharide degradation; Signal; Vacuole.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1879417"
FT CHAIN 27..299
FT /note="Hevamine-A"
FT /id="PRO_0000011952"
FT PROPEP 300..311
FT /note="Removed in mature form"
FT /id="PRO_0000011953"
FT DOMAIN 27..302
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 46..93
FT /evidence="ECO:0000269|PubMed:8831791,
FT ECO:0007744|PDB:2HVM"
FT DISULFID 76..83
FT /evidence="ECO:0000269|PubMed:8831791,
FT ECO:0007744|PDB:2HVM"
FT DISULFID 185..214
FT /evidence="ECO:0000269|PubMed:8831791,
FT ECO:0007744|PDB:2HVM"
FT VARIANT 296
FT /note="L -> R (in hevamine-B)"
FT VARIANT 306
FT /note="E -> K (in hevamine-B)"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1KQY"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2HVM"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2HVM"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2HVM"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2HVM"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2HVM"
SQ SEQUENCE 311 AA; 33718 MW; 2CEED8658A28C908 CRC64;
MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK YSYVNIAFLN
KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV MLSLGGGIGS YTLASQADAK
NVADYLWNNF LGGKSSSRPL GDAVLDGIDF DIEHGSTLYW DDLARYLSAY SKQGKKVYLT
AAPQCPFPDR YLGTALNTGL FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI
FLGLPAAPEA AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL
FLHSEECMTV L
