ID A0A0A2KDC1_PENIT Unreviewed; 1659 AA.
AC A0A0A2KDC1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PITC_018490 {ECO:0000313|EMBL:KGO65817.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65817.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65817.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65817.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO65817.1}.
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DR EMBL; JQGA01001473; KGO65817.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2KDC1; -.
DR HOGENOM; CLU_001837_4_0_1; -.
DR OMA; YCCPEKE; -.
DR OrthoDB; 50378at2759; -.
DR PhylomeDB; A0A0A2KDC1; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
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 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:SF401; CHITINASE; 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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 73..434
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1613..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1659 AA; 180971 MW; A5B384BECB1792A8 CRC64;
MPAAASVMDK VFVDMATSAI QTFVSATVMP LQPVEKMHLP QVQPAPSITD SGCQGDNCGS
PTVPSCSSND VLKRVIGYYE GWSNNRTCDS WSPSDLAVDG LTHLNYAFAT FDHDGDDWKV
SPMSGVADET EVINDLVNLK SNNPGLSVYL SIGGWSFNDG DTASYWSDMA SKASTRKSWA
KSVLFELKKY GFNGVDLDWE YPVATDRGGS PDDTKNYVSL ISELREVLDA SGTSYGISFT
TPASYWYLQY FDVPGMLSAG ADWTNIMTYD LHGVWDGTDP WIGKVMQAHT NLTEIKSALD
LMWRAGVEPS KIVMGTGFYG RSFTVDDPSC VDPGCAFSVA GNAGPCTATA GVLSYKEIVE
YMNYDDALVI LDDTAAVNYM VWDSATQWVS FDTNVTFQQK IKYANDVCLG GLMIWSLDQD
TYDWQALSGL LNKEVASGDL LTGGSMSDET AKDLATLYSA YTGTDCYVSD CVDVNKGQCK
SGYSVLEYVH SASLGMIEDP DKNLCKVGSD DSKDAQYRLI CCPTDAMPEG CCWEGGSDDG
SCTGGGTCGK GTYELVADSY ADRTGSNFCT SGKRSLCCNT DSALEKCDWT TCGNVCASDM
YTFSMETNFE GTNTYKNCEW YGCSDSCPSS KVLITQRTEI YSITEEGNDS VCSSGTNKLC
CDPPNGANSS PVDPKDLFTY PDEDDVSYYY NVQATSNEDA TSDDSKDPFA FVMIDGDTSA
YDESLVDQWT FLTDEQELSK RDLKHHKRES MFSNNNDTFD NVIETYHIQC TNLYVNVSNC
NSLFEGGASN TIVKMPKDLG AGPYARVISL VPLGSQSTSS NIKARSTSEV YELNVDYDLA
SAATEAKGDV NFRVDYTNLL EYWNEITDSP GSKRKRWFGA YDDWLKKMTA IVKDETSYLP
LDYEEKIKLF HAHANCPKTN IDATFDIDAN IKLALNGQYG YYFEGSILPT PTLISAYGYF
SIEPVAAILI TLRAEAVMQS DSGVIELFSA GFPGLSVKGL ISIGPELALT GQLSASLQVS
GELNAGVSLE WDRTEVYFPQ DAAGEKASIA PKDLQSDDNQ VYSFEPTFDA SLTAQGNLAL
SLTPEVRFGI SVLGGDLMSG YVTVGITNTI KLGVNATASV SGDGSTSAGF CYWADFVYSI
FIQANASFID GAAYWGDKYD VVSLSDPLPL VEETCIKYAS SDPLTKRDNV EALVANSTGS
GCFGGLIACN TVNDDTDSSG NMTCPYACEG TSCTILDTSS SLSRRQAVTG QCMHYPAMFY
NCEWFPNKDI PNLDTSTNGN MPYYSSLGIC TNIQNYLDRH ASLWAPSYMG DTWMRLTYKP
DPSNTNRNQA CGDPKKKTSN MAAHCAQVKR SLWPQAVQQA GKNAGGLQGW SESMSCDEFP
FNSAAEGGTG ASTSCTPWEQ QQYQSSITNM IPILHDRTNN NLPWSTEPWT GQLPRQYTVN
LFDSTSNPTG TFLGTYGGYL AGNQNLIRAR IAGGVNTFGT NSIYYLTATS HNALCHIDDG
FNLRSTAMGV KYIKLIVCNV VYGDSLGTDL KKRDGEDDDN YTGRPEMHPG FWQVQELRVP
KNWQNHVVLT RRGDSESFAR GLAHGSGASH GLKWDDTDSH ALHLLDENDQ RVQSSTLATR
AQGQAIPESE GESDVDLSAS ASWRKHYGEH LRRHGHGHH
//
