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CHID_NIACI
ID   CHID_NIACI              Reviewed;         524 AA.
AC   P27050;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 4.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Chitinase D;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chiD;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-42.
RC   STRAIN=WL-12;
RX   PubMed=1729234; DOI=10.1128/jb.174.2.408-414.1992;
RA   Watanabe T., Oyanagi W., Suzuki K., Ohnishi K., Tanaka H.;
RT   "Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and
RT   possible homology of the enzyme to other prokaryotic chitinases and class
RT   III plant chitinases.";
RL   J. Bacteriol. 174:408-414(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Watanabe T.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; D10594; BAA34114.1; -; Genomic_DNA.
DR   PIR; A41961; A41961.
DR   AlphaFoldDB; P27050; -.
DR   SMR; P27050; -.
DR   CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF51055; SSF51055; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:1729234"
FT   CHAIN           31..524
FT                   /note="Chitinase D"
FT                   /id="PRO_0000011906"
FT   DOMAIN          95..180
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          190..514
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        303
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   524 AA;  55760 MW;  208D714902A741E6 CRC64;
     MNQAVRFRPV ITFALAFILI ITWFAPRADA AAQWQAGTAY KQGDLVTYLN KDYECIQPHT
     ALTGWEPSNV PALWKYVGEG TGGGTPTPDT TPPTVPAGLT SSLVTDTSVN LTWNASTDNV
     GVTGYEVYRN GTLVANTSTT TAVVTGLTAG TTYVFTVKAK DAAGNLSAAS TSLSVTTSTG
     SSNPGPSGSK WLIGYWHNFD NGSTNIKLRN VSTAYDVINV SFAEPISPGS GTLAFTPYNA
     TVEEFKSDIA YLQSQGKKVL ISMGGANGRI ELTDATKKRQ QFEDSLKSII STYGFNGLDI
     DLEGSSLSLN AGDTDFRSPT TPKIVNLING VKALKSHFGA NFVLTAAPET AYVQGGYLNY
     GGPWGAYLPV IHALRNDLTL LHVQHYNTGS MVGLDGRSYA QGTADFHVAM AQMLLQGFNV
     GGSSGPFFSP LRPDQIAIGV PASQQAAGGG YTAPAELQKA LNYLIKGVSY GGSYTLRQPA
     GYVGLKGIMT WSINWDAYTN NQFSNAHRPF LNGLSTQKTE EVVY
 
 
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