ID A0A165ACF8_XYLHT Unreviewed; 1169 AA.
AC A0A165ACF8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=L228DRAFT_284976 {ECO:0000313|EMBL:KZF20249.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF20249.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF20249.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF20249.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(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. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; KV407463; KZF20249.1; -; Genomic_DNA.
DR RefSeq; XP_018185804.1; XM_018336285.1.
DR AlphaFoldDB; A0A165ACF8; -.
DR STRING; 1328760.A0A165ACF8; -.
DR GeneID; 28901422; -.
DR InParanoid; A0A165ACF8; -.
DR OMA; CWTGHKS; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
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; cd06922; ChtBD1_GH18_1; 1.
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 InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
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 PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
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:UP000076632};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1169
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007855240"
FT DOMAIN 68..120
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 121..480
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 85..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 90..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1169 AA; 124643 MW; 187A2E3E112598FB CRC64;
MQLLRLIAGC AILSLPVSAL LADDPSSDPY SCSASKPCKI GCCSKTGVCG LGPQFCGSDV
CISSCDAKSE CDPGWGAQWS NKEGCPLNVC CSKYGFCGTT SEFCGSKKVA EPSCGGNSAS
QKVIGYYEGW SSTRQCRGMY PEDLLLTAYT HMNYAFAFVD PNSFAVAPMS AGDTELYPRF
TALKKYNPGL QTWISIGGWS MNDPDQPTAA TFSNLAGSAD AQSKFFKSLV NFMSTYGFDG
VDIDWEYPVA PERSGKPADF ANYVSFLKNL KNALGSGGHN YGLTITLPSS YWYMQNFDIK
SIEPIVDWFN VMTYDLHGTW DSTDPYIGAV VNAHTNLTEI TQTFDLLWRN SIDPSKVVMG
MGFYGRSFTL SDPSCNTAGC PFSSGGNPGP CSASAGTLMY SEIEDIVSAG ATVTEDKDAG
VAIVTWGGNQ WVSYDNADTL KQKMDYANGK CLGGVMIWAA STDDASGTAI KALTGAAGRN
TFTEAALFNW PKKPIGQCVW GDCDAGCPTG FQPATGTGGK VSGYAGIFNG CKKGSSRYYC
CPTGSAPKCE WKGTAPFCGA TSGGRCSDNE VEVTTSTSAT GHTCWTGHKS LCCSHTDSDN
TLGQCSWEGS APFCTTAGVL LSPGVFFTSA NCPSDKPNKQ TTSKYGPGGD KPCLYDGGWK
SYCCANPNPW ANSHCAWHQG TADSWTGWAQ SWIAGGLAHG ILAPVLGTDC KGECPAGQVP
IATDGTSCQP GTYSYYCCDN PNAPALPAPG DISLCPSPPG LPGRNSGPDP DGSAPHIYAE
ADDFDGDCTL YALSSSTSKL KARDLDTLTI EDVRRWEQDL LTIKLSSNGG EVLLNDFWEP
EFDSDEPLSE NNHSLEARSL LAKRTLDKGS KLKFCSPGQP DIYMYPQTYS GYRTIARLAN
KGWITIAKPA ICGAIGVASL LTQPNNEDFV TEHVFEKQSL RNAIQYMTNG KLPGGGALSA
GKAAVTGVFD ATGAFFSNWP SALTPSFGDT PQATAFGALG HAQAPADYAN LQVCDADLNA
IKERIVAGIT FLSSDKWKAF GELEKVSYLS DVIDTFSYMR YTQTAQSYNA AYKSLVSFWS
LFSSHPSAQA GYDYVGAFKQ IVSADIDNQV STATTLFKTY LQDAISIWND PSITGVHPAS
VVTENQDALA DFLKNIGTYI SLDKLTMTS
//
