ID   CHIT2_TULSB             Reviewed;         275 AA.
AC   Q7M443;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Chitinase 2;
DE            EC=3.2.1.14;
DE   AltName: Full=Tulip bulb chitinase-2;
DE            Short=TBC-2;
OS   Tulipa saxatilis subsp. bakeri (Tulip) (Tulipa bakeri).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Tulipa.
OX   NCBI_TaxID=110455;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Bulb;
RX   PubMed=9692212; DOI=10.1271/bbb.62.1253;
RA   Yamagami T., Ishiguro M.;
RT   "Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus
RT   Tulipa.";
RL   Biosci. Biotechnol. Biochem. 62:1253-1257(1998).
CC   -!- FUNCTION: Able to cleave glycolchitin. {ECO:0000269|PubMed:9692212}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   PIR; JE0184; JE0184.
DR   AlphaFoldDB; Q7M443; -.
DR   SMR; Q7M443; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000677; Chitinase-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   PRINTS; PR00551; 2SGLOBULIN.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..275
FT                   /note="Chitinase 2"
FT                   /id="PRO_0000077048"
FT   DOMAIN          1..270
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   275 AA;  30863 MW;  760B7BAB1ADEE944 CRC64;
     ALFREYIGAQ FNDVKFSDVP INPNVDFHFI LAFAIDYTSG SSPTPTNGNF NPFWDTNNLS
     PSQVAAIKRT YNNVKVSVSL GGNSVGGERV FFNPSSVSSW VDNAVSSLTK IIKQYHLDGI
     DIDYEHFKGD PNTFAECIGQ LVTRLKKNGV VSFVSIAPFD DAQVQSHYQA LWEKYGHQID
     YVNFQFYVYS SRMSVEQFLK YFEMQRSNYP GGKVLVSFST DNSGGLKPRN GFFDACSILK
     KQGKLHGIFV WSADDSLMSN DVFKYEMQAQ SLLAS