ID A0A1E3QBS4_LIPST Unreviewed; 410 AA.
AC A0A1E3QBS4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN ORFNames=LIPSTDRAFT_42376 {ECO:0000313|EMBL:ODQ75028.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ75028.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ75028.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ75028.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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 Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000256|RuleBase:RU004453}.
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DR EMBL; KV454291; ODQ75028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3QBS4; -.
DR STRING; 675824.A0A1E3QBS4; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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 Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
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:UP000094385};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..410
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009134169"
FT DOMAIN 24..312
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 369..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODQ75028.1"
FT NON_TER 410
FT /evidence="ECO:0000313|EMBL:ODQ75028.1"
SQ SEQUENCE 410 AA; 42992 MW; D16819F59C4EDED1 CRC64;
LIFLASQICL FARPAYAYSS SSSDNVVVYW GQASAGSQQP LSYYCQSNSV DIVVLSFLMT
FYAADGLPEV NFANACSDTF SGTTLLQCDT IAQDIQTCQS MGKKVLLSLG GAAGLYGFSS
DSEGSSFATT LWNMFGGGTS DYRPFDTAVI DGFDLDIENG NSVGYAAFVK QMRSLYNGGD
YYISGAPQCP FPDASIGDAL DNAWFDFVFI QFYNNYCGVN NPSQFNYDSD WQSWVSSTAI
NKDVKLYVGV PGSSSAAGSG YSTPSALLDI INGISDKSSL GGVMIWDASQ AFANTVDSLL
FIDGIKDMLG QIGSSTSSTS DSSASSSVSS KLAVATSSGA VVSSESLAIT FSQAAQNLYV
DSSTTSQAVQ DPSTSSVAFE PTASTVSNPT SSIVEVPTSS ILEQSTSSTI
//