ID   CHI1_RHIOL              Reviewed;         540 AA.
AC   P29026;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Chitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI1;
OS   Rhizopus oligosporus (Rhizopus microsporus var. oligosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-52.
RC   STRAIN=ATCC 22959 / CBS 338.62 / NBRC 8631 / NRRL 2710 / AS 3.4818;
RX   PubMed=1429462; DOI=10.1128/jb.174.22.7398-7406.1992;
RA   Yanai K., Takaya N., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RT   "Purification of two chitinases from Rhizopus oligosporus and isolation and
RT   sequencing of the encoding genes.";
RL   J. Bacteriol. 174:7398-7406(1992).
CC   -!- FUNCTION: Probably involved in the apical growth and branching of
CC       fungal hyphae.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class III subfamily. {ECO:0000305}.
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DR   EMBL; D10157; BAA01021.1; -; Genomic_DNA.
DR   PIR; A47022; A47022.
DR   AlphaFoldDB; P29026; -.
DR   SMR; P29026; -.
DR   CAZy; CBM19; Carbohydrate-Binding Module Family 19.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   CLAE; CHI18A_RHIOL; -.
DR   GO; GO:0005576; C:extracellular region; 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:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR005089; CBM_fam19.
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; PF03427; CBM_19; 1.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1429462"
FT   CHAIN           23..417
FT                   /note="Chitinase 1"
FT                   /id="PRO_0000011930"
FT   PROPEP          418..540
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000011931"
FT   DOMAIN          29..314
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          314..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..404
FT                   /note="Chitin-binding, high affinity"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   540 AA;  56227 MW;  C7A8590D03881F1B CRC64;
     MLARTFLGMA ISAFLASTGV QAAWSSNGPN VMYYWGQNSA GGSNTQASLG TYCESGQVDA
     VLLSFLHVFN VGGTPEINLS SACAGTYFPN TQLLSCPAVG ADIKKCQDKG VKVILSLGGA
     AGVYGFTSDA QGQQFAQTIW NLFGGGSSDT RPFGDAVIDG VDLDIEGGAS TGYAAFVNAL
     RQKFSSNFLI GAAPQCPFPD AILGSVLNSA SFDYVNVQFY NNYCSATGSS FNFDTWDNWA
     KTTSPNKNVK IMFTIPGSPT AAGSGYVPMS TLQTIVPSLA SEYSSYGGVS VWDASQAWNN
     GDFSSQLYSL VHSGGSTPPP SSSTIKTTTK ATTTSTKTTT TAAPTATSAP GSCPVANQSC
     STQNQYACTA DGKYAVCDHG KWVVSSCPSG TVCIPTTDGT SIYCGYATGS GSTCPSASAL
     EIAAASFGSK NGPVPRPYKA SKVAAQLAVT STDKNSFEAV INARRTTLTP FEKSVTIEFT
     TPSNIKFTES DMGPVRQVGN KVRIQAKNDY NESMTLVVKV KGSINSGVFV APSTSAWKFK