ID   CHI5_PHAVU              Reviewed;         327 AA.
AC   P36361;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Endochitinase CH5B;
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 [GENOMIC DNA].
RC   STRAIN=cv. Saxa;
RX   PubMed=2535512; DOI=10.2307/3868947;
RA   Broglie K.E., Biddle P., Cressman R., Broglie R.;
RT   "Functional analysis of DNA sequences responsible for ethylene regulation
RT   of a bean chitinase gene in transgenic tobacco.";
RL   Plant Cell 1:599-607(1989).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; S43926; AAB23263.1; -; Genomic_DNA.
DR   PIR; JQ0965; JQ0965.
DR   RefSeq; XP_007137309.1; XM_007137247.1.
DR   AlphaFoldDB; P36361; -.
DR   SMR; P36361; -.
DR   STRING; 3885.XP_007137309.1; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   EnsemblPlants; ESW09303; ESW09303; PHAVU_009G116600g.
DR   GeneID; 18619862; -.
DR   Gramene; ESW09303; ESW09303; PHAVU_009G116600g.
DR   KEGG; pvu:PHAVU_009G116600g; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   OMA; GYGTITN; -.
DR   OrthoDB; 1132954at2759; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Signal; Vacuole.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..316
FT                   /note="Endochitinase CH5B"
FT                   /id="PRO_0000005313"
FT   PROPEP          317..327
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000005314"
FT   DOMAIN          27..67
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        29..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        38..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        61..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        96..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        169..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        276..308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   327 AA;  35291 MW;  5F13239464A9C7D8 CRC64;
     MKKNRMMIMI CSVGVVWMLL VGGSYGEQCG RQAGGALCPG GNCCSQFGWC GSTTDYCGKD
     CQSQCGGPSP APTDLSALIS RSTFDQVLKH RNDGACPAKG FYTYDAFIAA AKAYPSFGNT
     GDTATRKREI AAFLGQTSHE TTGGWATAPD GPYAWGYCFV RERNPSAYCS ATPQFPCAPG
     QQYYGRGPIQ ISWNYNYGQC GRAIGVDLLN KPDLVATDSV ISFKSALWFW MTAQSPKPSS
     HDVITSRWTP SSADVAARRL PGYGTVTNII NGGLECGRGQ DSRVQDRIGF FKRYCDLLGV
     GYGNNLDCYS QTPFGNSLFL SDLVTSQ