ID C8Z5T2_YEAS8 Unreviewed; 511 AA.
AC C8Z5T2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=EC1118_1D0_6667g {ECO:0000313|EMBL:CAY78871.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY78871.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY78871.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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; FN393063; CAY78871.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z5T2; -.
DR SMR; C8Z5T2; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR HOGENOM; CLU_002833_1_2_1; -.
DR Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..472
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 511 AA; 59118 MW; 238FF79963BF0D63 CRC64;
MVGHSAQHRS KSSLVSHLLI LLIFITIIIE MCLYNKIFKN QRSDDIRDNF NNGGHRVPSN
VQNHGTHIRD EAFISGVYYS NWSPYKPRFH FPHDINLKQV SHIYYAFFKI NSRTGGIENT
DSWSDLEMNL YKSLAIKNSE LIKESSNNSV QNILPLGCIG ELFYLKNTCS DKKFKVIMSI
GGWSDSENFK IIIKDDKLLQ NFVDSSVETM FRLGFDGIDL DWEFPGNNES EPRGYLKLVR
MLRLKLNSLE SQIFGKRTED HFQLSIAAPA FKDKLFYLPI TEIDQYVDYW NMMTYDYYGS
WSETTGYHSN LFSETELNGN FAMHYMIDRF GVNSRKLVLG MAAYGRSFHI KDNKFEPFNQ
NTVLINKIFK GVGKPTKEID KADGKEGIWP YKNLPKIGTI EQYDPKYVSA YCFDEKNSIF
ISYDNTKSVK TKAEYVTHNN LGGGFWWESC GEAYANESRS LINAFNEGLH FNVSSKPSIF
QDVRVKKYYL NKYGDGGFLS PYLKHLDSRK Q
//
