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Endochitinase (EC 3.2.1.14)

 CHIT_PHAVU              Reviewed;         328 AA.
P06215;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
22-NOV-2017, entry version 119.
RecName: Full=Endochitinase;
EC=3.2.1.14;
Flags: Precursor;
Phaseolus vulgaris (Kidney bean) (French bean).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Saxa;
PubMed=2428042; DOI=10.1073/pnas.83.18.6820;
Broglie K.E., Gaynor J.J., Broglie R.M.;
"Ethylene-regulated gene expression: molecular cloning of the genes
encoding an endochitinase from Phaseolus vulgaris.";
Proc. Natl. Acad. Sci. U.S.A. 83:6820-6824(1986).
[2]
PROTEIN SEQUENCE OF 28-57.
Lucas J., Henschen A., Lottspeich F., Voegeli U., Boller T.;
"Amino-terminal sequence of ethylene-induced bean leaf chitinase
reveals similarities to sugar-binding domains of wheat germ
agglutinin.";
FEBS Lett. 193:208-210(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-51.
PubMed=16665863; DOI=10.1104/pp.86.1.182;
Hedrick S.A., Bell J.N., Boller T., Lamb C.J.;
"Chitinase cDNA cloning and mRNA induction by fungal elicitor,
wounding, and infection.";
Plant Physiol. 86:182-186(1988).
-!- FUNCTION: Defense against chitin-containing fungal pathogens.
-!- CATALYTIC ACTIVITY: Random endo-hydrolysis of N-acetyl-beta-D-
glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. Note=Vacuolar and
protoplast. {ECO:0000250}.
-!- INDUCTION: By ethylene.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
class I subfamily. {ECO:0000305}.
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EMBL; M13968; AAA33756.1; -; mRNA.
EMBL; M19052; AAA33757.1; -; mRNA.
ProteinModelPortal; P06215; -.
SMR; P06215; -.
CAZy; CBM18; Carbohydrate-Binding Module Family 18.
CAZy; GH19; Glycoside Hydrolase Family 19.
PRIDE; P06215; -.
ProMEX; P06215; -.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
CDD; cd00325; chitinase_glyco_hydro_19; 1.
Gene3D; 3.30.60.10; -; 1.
InterPro; IPR001002; Chitin-bd_1.
InterPro; IPR018371; Chitin-binding_1_CS.
InterPro; IPR036861; Endochitinase-like_sf.
InterPro; IPR016283; Glyco_hydro_19.
InterPro; IPR000726; Glyco_hydro_19_cat.
InterPro; IPR023346; Lysozyme-like_dom_sf.
Pfam; PF00187; Chitin_bind_1; 1.
Pfam; PF00182; Glyco_hydro_19; 1.
PIRSF; PIRSF001060; Endochitinase; 1.
PRINTS; PR00451; CHITINBINDNG.
ProDom; PD000609; Chitin_bd_1; 1.
SMART; SM00270; ChtBD1; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF57016; SSF57016; 1.
PROSITE; PS00026; CHIT_BIND_I_1; 1.
PROSITE; PS50941; CHIT_BIND_I_2; 1.
PROSITE; PS00773; CHITINASE_19_1; 1.
PROSITE; PS00774; CHITINASE_19_2; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Chitin degradation; Chitin-binding;
Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
Plant defense; Polysaccharide degradation; Signal; Vacuole.
SIGNAL 1 27 {ECO:0000269|Ref.2}.
CHAIN 28 317 Endochitinase.
/FTId=PRO_0000005311.
PROPEP 318 328 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000005312.
DOMAIN 28 68 Chitin-binding type-1.
{ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 30 45 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 39 51 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 44 58 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 62 66 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 97 159 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 170 178 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 277 309 {ECO:0000255|PROSITE-ProRule:PRU00261}.
VARIANT 88 88 M -> V.
VARIANT 168 168 T -> A.
VARIANT 210 210 L -> F.
CONFLICT 40 40 P -> L (in Ref. 3; AAA33757).
{ECO:0000305}.
CONFLICT 54 54 T -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 D -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
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


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