CHIT_CARPA
ID CHIT_CARPA Reviewed; 243 AA.
AC P85084;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Endochitinase;
DE EC=3.2.1.14;
OS Carica papaya (Papaya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC TISSUE=Latex {ECO:0000269|PubMed:17115118};
RX PubMed=17115118; DOI=10.1007/s00018-006-6320-3;
RA Huet J., Wyckmans J., Wintjens R., Boussard P., Raussens V.,
RA Vandenbussche G., Ruysschaert J.M., Azarkan M., Looze Y.;
RT "Structural characterization of two papaya chitinases, a family GH19 of
RT glycosyl hydrolases.";
RL Cell. Mol. Life Sci. 63:3042-3054(2006).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. Shows
CC activity on chitin, tetra-N-acetylglucosamine and chitosan.
CC {ECO:0000269|PubMed:17115118}.
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 Evidence={ECO:0000269|PubMed:17115118};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P19171}.
CC Note=Vacuolar and protoplast. {ECO:0000250|UniProtKB:P19171}.
CC -!- MASS SPECTROMETRY: Mass=26534; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17115118};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000255}.
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DR PDB; 3CQL; X-ray; 1.50 A; A/B=1-243.
DR PDBsum; 3CQL; -.
DR AlphaFoldDB; P85084; -.
DR SMR; P85084; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR BRENDA; 3.2.1.14; 1191.
DR EvolutionaryTrace; P85084; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Plant defense; Polysaccharide degradation; Vacuole.
FT CHAIN 1..243
FT /note="Endochitinase"
FT /id="PRO_0000285971"
FT ACT_SITE 67
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 23..85
FT /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT DISULFID 97..105
FT /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT DISULFID 223..236
FT /evidence="ECO:0000250|UniProtKB:Q9FRV1"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:3CQL"
FT TURN 15..19
FT /evidence="ECO:0007829|PDB:3CQL"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:3CQL"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 50..67
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3CQL"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3CQL"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:3CQL"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:3CQL"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3CQL"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:3CQL"
SQ SEQUENCE 243 AA; 26541 MW; 51F48F5F9A722703 CRC64;
GIEKIISRSM FDQMLKHRNN PACPAKGFYT YDAFLAAAKS FPSFGTTGST DVRKRELAAF
LGQTSHETTG GWPSAPDGPY AWGYCFLKER NPSSNYCAPS PRYPCAPGKS YYGRGPLQLS
WNYNYGPCGE ALRVNLLGNP DLVATDRVLS FKTALWFWMT PQAPKPSCHD VLTGRWQPSA
ADTAAGRLPG YGVLTNLLNG GLECGKGPNP QVADRLGFFR RYCGLLGVGT GNNLDCYNQR
PFG