CHIS_STRSN
ID CHIS_STRSN Reviewed; 278 AA.
AC P33665;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Chitosanase;
DE EC=3.2.1.132;
DE Flags: Precursor;
GN Name=csn; Synonyms=chs;
OS Streptomyces sp. (strain N174).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=69019;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8125325; DOI=10.1016/0378-1119(94)90738-2;
RA Masson J.-Y., Denis F., Brzezinski R.;
RT "Primary sequence of the chitosanase from Streptomyces sp. strain N174 and
RT comparison with other endoglycosidases.";
RL Gene 140:103-107(1994).
RN [2]
RP PROTEIN SEQUENCE OF 41-57, AND CHARACTERIZATION.
RA Boucher I., Dupuy A., Vidal P., Neugebauer W.A., Brzezinski R.;
RT "Purification and characterization of a chitosanase from Streptomyces
RT N174.";
RL Appl. Microbiol. Biotechnol. 38:188-193(1992).
RN [3]
RP CHARACTERIZATION.
RA Fink D., Boucher I., Denis F., Brzezinski R.;
RT "Cloning and expression in Streptomyces lividans of a chitanase-encoding
RT gene from the actinomycete Kitasatosporia N174 isolated from soil.";
RL Biotechnol. Lett. 13:845-850(1991).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7487871; DOI=10.1042/bj3110377;
RA Fukamizo T., Honda Y., Goto S., Boucher I., Brzezinski R.;
RT "Reaction mechanism of chitosanase from Streptomyces sp. N174.";
RL Biochem. J. 311:377-383(1995).
RN [5]
RP MUTAGENESIS.
RX PubMed=8537367; DOI=10.1074/jbc.270.52.31077;
RA Boucher I., Fukamizo T., Honda Y., Willick G.E., Neugebauer W.A.,
RA Brzezinski R.;
RT "Site-directed mutagenesis of evolutionary conserved carboxylic amino acids
RT in the chitosanase from Streptomyces sp. N174 reveals two residues
RT essential for catalysis.";
RL J. Biol. Chem. 270:31077-31082(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8564542; DOI=10.1038/nsb0296-155;
RA Marcotte E.M., Monzingo A.F., Ernst S.R., Brzezinski R., Robertus J.D.;
RT "X-ray structure of an anti-fungal chitosanase from streptomyces N174.";
RL Nat. Struct. Biol. 3:155-162(1996).
CC -!- FUNCTION: Aids in the defense against invading fungal pathogens by
CC degrading their cell wall chitosan.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 46 family. {ECO:0000305}.
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DR EMBL; L07779; AAA19865.1; -; Genomic_DNA.
DR PDB; 1CHK; X-ray; 2.40 A; A/B=41-278.
DR PDBsum; 1CHK; -.
DR AlphaFoldDB; P33665; -.
DR BMRB; P33665; -.
DR SMR; P33665; -.
DR CAZy; GH46; Glycoside Hydrolase Family 46.
DR BRENDA; 3.2.1.132; 1284.
DR SABIO-RK; P33665; -.
DR EvolutionaryTrace; P33665; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00978; chitosanase_GH46; 1.
DR Gene3D; 3.30.386.10; -; 1.
DR InterPro; IPR000400; Glyco_hydro_46.
DR InterPro; IPR023099; Glyco_hydro_46_N.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF01374; Glyco_hydro_46; 1.
DR PIRSF; PIRSF036551; Chitosanase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS60000; CHITOSANASE_46_80; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 41..278
FT /note="Chitosanase"
FT /id="PRO_0000012209"
FT ACT_SITE 62
FT /note="Proton donor"
FT ACT_SITE 80
FT /note="Nucleophile"
FT MUTAGEN 62
FT /note="E->D,Q: Drastic reduction of activity."
FT /evidence="ECO:0000269|PubMed:8537367"
FT MUTAGEN 80
FT /note="D->E,N: Drastic reduction of activity."
FT /evidence="ECO:0000269|PubMed:8537367"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1CHK"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1CHK"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 219..236
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1CHK"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1CHK"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1CHK"
SQ SEQUENCE 278 AA; 29835 MW; AEB36286AA9AF95F CRC64;
MHSQHRTARI ALAVVLTAIP ASLATAGVGY ASTQASTAVK AGAGLDDPHK KEIAMELVSS
AENSSLDWKA QYKYIEDIGD GRGYTGGIIG FCSGTGDMLE LVQHYTDLEP GNILAKYLPA
LKKVNGSASH SGLGTPFTKD WATAAKDTVF QQAQNDERDR VYFDPAVSQA KADGLRALGQ
FAYYDAIVMH GPGNDPTSFG GIRKTAMKKA RTPAQGGDET TYLNAFLDAR KAAMLTEAAH
DDTSRVDTEQ RVFLKAGNLD LNPPLKWKTY GDPYVINS
