ID   CSNC_ASPOZ              Reviewed;         380 AA.
AC   Q75R32;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Endo-chitosanase C;
DE            EC=3.2.1.132;
DE   Flags: Precursor;
GN   Name=csnC;
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 100-121 AND 185-214,
RP   DOMAIN, CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=IAM2660;
RX   PubMed=22232262; DOI=10.1271/bbb.110605;
RA   Sugita A., Sugii A., Sato K., Zhang X.-Y., Dai A.-L., Taguchi G.,
RA   Shimosaka M.;
RT   "Cloning and characterization of a gene coding for a major extracellular
RT   chitosanase from the koji mold Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 76:193-195(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=IAM2660;
RX   PubMed=11055393; DOI=10.1271/bbb.64.1896;
RA   Zhang X.Y., Dai A.L., Zhang X.K., Kuroiwa K., Kodaira R., Shimosaka M.,
RA   Okazaki M.;
RT   "Purification and characterization of chitosanase and Exo-beta-D-
RT   glucosaminidase from a Koji mold, Aspergillus oryzae IAM2660.";
RL   Biosci. Biotechnol. Biochem. 64:1896-1902(2000).
CC   -!- FUNCTION: Chitosanase catalyzing the endo-type cleavage of chitosan,
CC       the deacylated form of chitin. Chitosanase may be crucial in the
CC       degradation of the deacetylated portion of chitin in the fungal cell
CC       wall. Chitoolisaccharides produced by the hydrolysis of partially N-
CC       acetylated chitosan are known to have many biological activities,
CC       including antibacterial activity, immune-enhancing effects, and
CC       elicitor activity. {ECO:0000269|PubMed:11055393,
CC       ECO:0000269|PubMed:22232262}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC         Evidence={ECO:0000269|PubMed:11055393, ECO:0000269|PubMed:22232262};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:11055393};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:11055393};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22232262}.
CC   -!- DOMAIN: The C-terminal R3 domain contains 3 tandem repeats required for
CC       the binding to insoluble chitosan. {ECO:0000269|PubMed:22232262}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 75 family. {ECO:0000305}.
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DR   EMBL; AB159785; BAD08218.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q75R32; -.
DR   SMR; Q75R32; -.
DR   STRING; 5062.CADAORAP00011439; -.
DR   CAZy; GH75; Glycoside Hydrolase Family 75.
DR   CLAE; CSN75C_ASPOR; -.
DR   VEuPathDB; FungiDB:AO090113000063; -.
DR   eggNOG; ENOG502S39Y; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR009939; Chitosanase_fungal.
DR   PANTHER; PTHR42061; PTHR42061; 1.
DR   Pfam; PF07335; Glyco_hydro_75; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..380
FT                   /note="Endo-chitosanase C"
FT                   /id="PRO_0000429639"
FT   REPEAT          276..304
FT                   /note="R3-1"
FT   REPEAT          311..341
FT                   /note="R3-2"
FT   REPEAT          348..378
FT                   /note="R3-3"
SQ   SEQUENCE   380 AA;  38952 MW;  A8658467AF55FA0C CRC64;
     MPIKSFASRL ALSLAICGTA MGQKVNGADY NKPDGGPPAK FFQASSSIPV AAIQAAAAKA
     SKVPSHATYP IGQGSTKSTI HSDWAGFSEG AAFSFIADMD VDCDGLNHGC KGNPDGQKET
     NWGALSAYEV PFIVIPQEFL DANKGTLKGN AVAAVICNGK MFYGIFGDSN GDSPQVTGEA
     SWLMARTCFP KEDLNGNKGH TAADVTYIVF TGDKAVLPSS ALNKNYITNF DTLRSMGDSL
     VGALAKNLNL GGGGGNPPTT LTTTSIPEPT GGSGSCSWPG HCAGATCSSN DDCSDDLTCQ
     NGKCASDGSA ETCSWEGHCK GATCSSNDDC SDELACISGI CSVDNGVETC EWEGHCEGAS
     CSSHDDCDGN LACKNGKCSA