ID   CHI1_CANAX              Reviewed;         462 AA.
AC   P46876;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHT1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX   PubMed=8740424;
RX   DOI=10.1002/(sici)1097-0061(199604)12:5<501::aid-yea931>3.0.co;2-u;
RA   McCreath K.J., Specht C.A., Liu Y., Robbins P.W.;
RT   "Molecular cloning of a third chitinase gene (CHT1) from Candida
RT   albicans.";
RL   Yeast 12:501-504(1996).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Specht C.A.;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
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DR   EMBL; U36490; AAC49409.2; -; Genomic_DNA.
DR   AlphaFoldDB; P46876; -.
DR   SMR; P46876; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   VEuPathDB; FungiDB:CAWG_04786; -.
DR   VEuPathDB; FungiDB:CR_00180C_A; -.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008843; F:endochitinase activity; IEA:EnsemblFungi.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-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   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..462
FT                   /note="Chitinase 1"
FT                   /id="PRO_0000011924"
FT   DOMAIN          18..291
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   462 AA;  48916 MW;  978515D7ABECABCD CRC64;
     MILNLIILLA ISIVASASNI AAYWGQNAGG DQQTLGDYCS SSPASIIILS FLDGFPNLSL
     NFANQCSGTF SSGLAHCSQI GSDIKSCQQQ GKTILLSLGG ATGNYGFSSD SEAVQFAGTL
     WNKFGGGKDS ERPFDDAIVD GFDFDIENKD QTGYAALATQ LRKYFSTGTK SYYLSAAPQC
     PYPDESVGDL MSQVDLDFAF IQFYNNYCSL NQQFNWNSWS NYARGKSIKL YLGLPGSSSS
     AGSGFVGLST VQRVVASIKG DSSFGGISIW DISSAENGGY LNQLYQALSG SGSPAAPSNS
     YQPNTPLTRT YGGSTATASA YISVGFTAGA THGSTTTNDL LAWIDSLFGS SQSSVQQYAT
     PVQSVTATPQ PVAATTTSAP KPTASAFNWF GWFDGTTTST TLQTVYSTVP ADQTVYVTLT
     TTVGSQMLQS LFDKRDVIAE AKSTNLQICW LLFIPLLALI CS