ID G7XZD1_ASPKW Unreviewed; 1277 AA.
AC G7XZD1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=AKAW_10388 {ECO:0000313|EMBL:GAA92274.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA92274.1};
RN [1] {ECO:0000313|EMBL:GAA92274.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92274.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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DR EMBL; DF126491; GAA92274.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XZD1; -.
DR STRING; 1033177.G7XZD1; -.
DR VEuPathDB; FungiDB:AKAW_10388; -.
DR eggNOG; KOG2806; Eukaryota.
DR InParanoid; G7XZD1; -.
DR Proteomes; UP000006812; 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; cd00035; ChtBD1; 1.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1277
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003506149"
FT DOMAIN 315..360
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 379..427
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 523..898
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1277 AA; 137353 MW; 2830D9F8DAEEDCD1 CRC64;
MGSNMALLSF LCILIQVAAL AAAASFNSSV RVTDPYIATQ WNACPSICDS ANPNDWDFYP
NLRILKSCKE PMLLNLMVGF PNSTTNLNPR QPLYACSTTN NGYNSATSKA KVASTPNASS
SRYLNKDVQV ETAWRGEETS RYTSHTGVAA QLVQSQLNAP SSKNATIAIG YSNGVVLGAF
VGSKIQKGSD NDGILGLFQN KIQQGELNKS GVMMQVCESD RAAAYTLGVI AEASPDSSRA
LSAVREALAT WDTGKCVSGY SGSSTSTISV GEVVDEGQND GPISGGNGTS VHRRAHKHSH
GKGLLHEKHR RATCTAIQVN DGDSCSKLAS RCGISPADFT KYNPSSTLCS SLLAGQHVCC
SAGTLPDYSP QPNADGTCAT YNIQNNDGCS KIAAAKSITV NDIKEWNKKS WGWTGCDNIQ
AGANICVSKG DPPMPSTLKN AVCGPQKPGT KRPDNWDDIE SLNPCPLNAC CDIWGQCGTT
AEFCTKTSST TDAPGTAKDG TNGCISNCGT DIVFDGNGFD DHPVLVGYYE AFQNSRPCLN
LDVTAINNTV QWGGQQGSHS STFSQAWDHI HFAFANITES FEVDVSSVQD EFEQFRKFKS
AGKKPKVLSF GGWSFSTDLD SYAIFRKGVT DEQRSLFASN VAKFADDNDL DGLDFDWEYP
GAPDIPGIPA GDPGDGDRYL QFLKEVRDKL SSEKTLSIAA PASYWYLKGF PIANISSVVD
YIVYMTYDLH GQWDWDNAWS VDGCDGGGCL RSHVNYTEIV NSLSMITKAG VPNSKIVAGL
ASYGRSFGMV DPSCYGPECK FKGPESAAMP GECTQTPGYI ANAEINDWLH GDQNITTYFD
HVSRSTISYS ANGTWVAYTD DNERNNRITE WWYNRTVLGT SLWAIDLTEF VAELPDGTVL
PPLTLPNCDQ AFTSLDDVEA SADSIDPECM NLYLIQALKS NLSSSVSAYH DVMKTDYDKK
FGWYQDAVRE QFPRSLQAFL KANASNYFEC TSQGMVPRSE EPEGKNVSSS CPSNPKDTGY
AIFYWTATDK DGFLEDLEDT TGISPDQLVW EIDASQCVSS PDPSQPMICS GSRNIGMPTL
PPDFTVSNPK DIISARLPNI TTFEEQSTTI ATLADSDLYL GDTIDVVDGA SLLVLMVSNS
IASMKSVESI GEEYHKEQVE EAILLFVTAF LLLIPGIGEL ADSVELTSVA VTLRAIGAAG
DAGFGIYSVV SAKDAGAGEI FLALLGGLGI LDMLEAPALF AKAAKARRAM DAGDIAKLGD
EVKGGMAQID KLKQLCR
//
