ID   CSN_ASPOR               Reviewed;         245 AA.
AC   Q2U3M5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Endo-chitosanase;
DE            EC=3.2.1.132;
DE   Flags: Precursor;
GN   Name=csn; Synonyms=csnA; ORFNames=AO090020000697;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 75 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007167; BAE63840.1; -; Genomic_DNA.
DR   PIR; JC7659; JC7659.
DR   RefSeq; XP_001824973.1; XM_001824921.1.
DR   AlphaFoldDB; Q2U3M5; -.
DR   CAZy; GH75; Glycoside Hydrolase Family 75.
DR   EnsemblFungi; BAE63840; BAE63840; AO090020000697.
DR   GeneID; 5997059; -.
DR   KEGG; aor:AO090020000697; -.
DR   VEuPathDB; FungiDB:AO090020000697; -.
DR   HOGENOM; CLU_046555_0_0_1; -.
DR   OMA; SGDNGHD; -.
DR   Proteomes; UP000006564; Chromosome 6.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..245
FT                   /note="Endo-chitosanase"
FT                   /id="PRO_0000429636"
SQ   SEQUENCE   245 AA;  26478 MW;  085E5B342F6C6CD8 CRC64;
     MHFAGIVAIA LATGATAYDL PENLKQIYEK HKSGKCSKEL QGGYDNGHSH DGKSFSYCGD
     IPNAIYLHSS KNGGQYADMD IDCDGANRHA GKCSNDHSGQ GETRWKDEVQ KLGIDDLDAN
     IHPYVVFGNE NDDGDDPEFD PRKHGMEPLS VMAVVCNKKL FYGIWGDTNG HTATGEASLS
     MAELCFPEED PSGDSGHEPN DVLYIGFTGK EAVPGKSADW KADSTESFEE SIKELGDKLV
     AGLKA