ID W5WPG3_9PSEU Unreviewed; 562 AA.
AC W5WPG3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=KALB_6716 {ECO:0000313|EMBL:AHI00075.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00075.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00075.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00075.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; CP007155; AHI00075.1; -; Genomic_DNA.
DR RefSeq; WP_025359950.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WPG3; -.
DR STRING; 1449976.KALB_6716; -.
DR KEGG; kal:KALB_6716; -.
DR PATRIC; fig|1449976.3.peg.6743; -.
DR eggNOG; COG3469; Bacteria.
DR HOGENOM; CLU_019399_1_1_11; -.
DR OrthoDB; 5172397at2; -.
DR Proteomes; UP000019225; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_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 PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..562
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004875598"
FT DOMAIN 175..257
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 269..562
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 163..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 56643 MW; 677097BA37EE5D73 CRC64;
MTRTKRLLAV LTAAALTALG VALSPAGSAH AAANLLANSG FEAGNTAGWT CNGAAVVGSP
THSGSYAVAA TPAGSDYAQC SQKITVLPNS AYTLTAWVQG SYVYLGATGT GGTDPSTWTS
SSGYTQLSTS FTTGASTTSV TIYVHGWFGQ PTYYADDLVL SGPGGGGGDT QPPSAPTGLT
ATGTTSSSTS LSWSAPSGSV SGYNVYQGGT KIASTTGTTY AVSGLSASTA YSFAVSAYNT
AGESARSAAV SVTTQSGGGN PGGGSLPAHV LTGYWQNFYN GAKALKLADV PTSYDLVAVA
FADTDPSKPG GVTFTLDSGL SSQLGGYTDA QFTADVQALH ARGQKVIISV GGQNGTVSVG
DATAANNFAA SVYALMQRYG FDGVDIDLEN GVNPTYMGQA LHSLAAKAGS GFVLTMAPET
IGMQSTGMAY FQLALNVKDI LTIVNTQFYN SGTMNGCDGN VYAQSTVNFL TALSCIQLQG
GLRADQVGLG LPATSSAAGG GYQSPSNVNN ALDCLAKGTN CGSFKPATTY PGIRGAMTWS
INWDASNGYA FANTVHPHLG TL
//
