CHIT_PHAVU
ID CHIT_PHAVU Reviewed; 328 AA.
AC P06215;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Endochitinase;
DE EC=3.2.1.14;
DE Flags: Precursor;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Saxa;
RX PubMed=2428042; DOI=10.1073/pnas.83.18.6820;
RA Broglie K.E., Gaynor J.J., Broglie R.M.;
RT "Ethylene-regulated gene expression: molecular cloning of the genes
RT encoding an endochitinase from Phaseolus vulgaris.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6820-6824(1986).
RN [2]
RP PROTEIN SEQUENCE OF 28-57.
RA Lucas J., Henschen A., Lottspeich F., Voegeli U., Boller T.;
RT "Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals
RT similarities to sugar-binding domains of wheat germ agglutinin.";
RL FEBS Lett. 193:208-210(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-51.
RX PubMed=16665863; DOI=10.1104/pp.86.1.182;
RA Hedrick S.A., Bell J.N., Boller T., Lamb C.J.;
RT "Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding,
RT and infection.";
RL Plant Physiol. 86:182-186(1988).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. Note=Vacuolar and
CC protoplast. {ECO:0000250}.
CC -!- INDUCTION: By ethylene.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; M13968; AAA33756.1; -; mRNA.
DR EMBL; M19052; AAA33757.1; -; mRNA.
DR AlphaFoldDB; P06215; -.
DR SMR; P06215; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR ProMEX; P06215; -.
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 Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Plant defense; Polysaccharide degradation; Signal; Vacuole.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 28..317
FT /note="Endochitinase"
FT /id="PRO_0000005311"
FT PROPEP 318..328
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000005312"
FT DOMAIN 28..68
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 30..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 39..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 62..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 97..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 170..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 277..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT VARIANT 88
FT /note="M -> V"
FT VARIANT 168
FT /note="T -> A"
FT VARIANT 210
FT /note="L -> F"
FT CONFLICT 40
FT /note="P -> L (in Ref. 3; AAA33757)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 35444 MW; 0B5A73626C776C8A CRC64;
MKKNRMMMMI WSVGVVWMLL LVGGSYGEQC GRQAGGALCP GGNCCSQFGW CGSTTDYCGP
GCQSQCGGPS PAPTDLSALI SRSTFDQMLK HRNDGACPAK GFYTYDAFIA AAKAYPSFGN
TGDTATRKRE IAAFLGQTSH ETTGGWATAP DGPYAWGYCF VRERNPSTYC SATPQFPCAP
GQQYYGRGPI QISWNYNYGQ CGRAIGVDLL NKPDLVATDS VISFKSALWF WMTAQSPKPS
SHDVITSRWT PSSADVAARR LPGYGTVTNI INGGLECGRG QDSRVQDRIG FFKRYCDLLG
VGYGNNLDCY SQTPFGNSLL LSDLVTSQ
