ID   Q9EY44_CELUD            Unreviewed;       571 AA.
AC   Q9EY44;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Chitinase A {ECO:0000313|EMBL:AAG27061.2};
GN   Name=chiA {ECO:0000313|EMBL:AAG27061.2};
OS   Cellulomonas uda.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1714 {ECO:0000313|EMBL:AAG27061.2};
RN   [1] {ECO:0000313|EMBL:AAG27061.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 21399 {ECO:0000313|EMBL:AAG27061.2};
RX   PubMed=14586544; DOI=10.1007/s00203-003-0611-y;
RA   Reguera G., Leschine S.B.;
RT   "Biochemical and genetic characterization of ChiA, the major enzyme
RT   component for the solubilization of chitin by Cellulomonas uda.";
RL   Arch. Microbiol. 180:434-443(2003).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; AY008839; AAG27061.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EY44; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489}.
FT   DOMAIN          50..158
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          203..571
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  59150 MW;  150C54AAB51292DD CRC64;
     MPHFPSHRSK HHHPPAAGDG AGPHTAATTR ALSRCRSRGA VATGLVAAFP ATAAGPFTAT
     FTSAGDWGTG HQASVTVTNG TTSTASTWTL EFDLPAGTTI TSSWDADVTR TGTHYKVTSK
     SWAGPFAPGA TQTWGYIGSG PFAQPTGCTV NGATCTGGTV PTNPTTGPTT NPTTGPTTNP
     TTGPTTNPTT GPTSNPTANP GGRKLVGYFA EWGVYGRNYH VNNIRTSGSA SKLTHILYAF
     GNTTGGRCSI GDAYAAYDKA YTADQSVDGV ADTWDQPLRG NFNQLRKLKA ANPGLKVLWS
     FGGWTWSGGF TQAAANPTAF ADSCYSLLND PRWAGLFDGI DVDWEYPNAC GLSCDSSGPQ
     AFDRVVTALR DKFGSSFLVT AAITADGSSG GKIDATDYAT AATKLSWIMP MTYDYFGAFN
     PQGPTAPHSP LTSYPGIPQA GFNSEDAVNK LIAKGIPASK ILLGVGFYGR GWTGVTQSAP
     GGSATGAAPG TYEAGIEDYK VLKNRCPATG TVGGTAYAKC GNEWWSYDTP ATIATKTAWA
     RSKGLGGAFF WELSGDTSNG ELVSALSRVS A
//