ID   CHIT1_TULSB             Reviewed;         314 AA.
AC   Q9SLP4; Q7M444;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Chitinase 1;
DE            EC=3.2.1.14;
DE   AltName: Full=Tulip bulb chitinase-1;
DE            Short=TBC-1;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ENZYME ACTIVITY.
RX   PubMed=10945255; DOI=10.1271/bbb.64.1394;
RA   Yamagami T., Tsutsumi K., Ishiguro M.;
RT   "Cloning, sequencing, and expression of the tulip bulb chitinase-1 cDNA.";
RL   Biosci. Biotechnol. Biochem. 64:1394-1401(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-301, 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:10945255,
CC       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         Evidence={ECO:0000269|PubMed:10945255};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AB035668; BAA88408.1; -; mRNA.
DR   PIR; JC7335; JC7335.
DR   PIR; JE0183; JE0183.
DR   AlphaFoldDB; Q9SLP4; -.
DR   SMR; Q9SLP4; -.
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; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:9692212"
FT   CHAIN           27..314
FT                   /note="Chitinase 1"
FT                   /id="PRO_0000011920"
FT   DOMAIN          27..296
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   314 AA;  35091 MW;  AE9F5D31522A03E7 CRC64;
     MASVSPSSLL LLFFALLSPL LPLTSALVFR EYIGSQFNDV KFSDVPINPD VDFHFILAFA
     IDYTSGSSPT PTNGNFKPFW DTNNLSPSQV AAVKRTHSNV KVSLSLGGDS VGGKNVFFSP
     SSVSSWVENA VSSLTRIIKQ YHLDGIDIDY EHFKGDPNTF AECIGQLVTR LKKNEVVSFV
     SIAPFDDAQV QSHYQALWEK YGHQIDYVNF QFYAYSARTS VEQFLKYFEE QSSNYHGGKV
     LVSFSTDSSG GLKPDNGFFR ACSILKKQGK LHGIFVWSAD DSLMSNNVFR YEMQAQSMLA
     SVNSRDRAMY WSLL