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