ID A0A0A2KZJ1_PENIT Unreviewed; 1057 AA.
AC A0A0A2KZJ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PITC_003610 {ECO:0000313|EMBL:KGO73174.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73174.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73174.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73174.1,
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:KGO73174.1}.
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DR EMBL; JQGA01000835; KGO73174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KZJ1; -.
DR STRING; 40296.A0A0A2KZJ1; -.
DR HOGENOM; CLU_001482_1_0_1; -.
DR OMA; AMQLCGP; -.
DR OrthoDB; 11640at2759; -.
DR PhylomeDB; A0A0A2KZJ1; -.
DR Proteomes; UP000030104; 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 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; IPR029226; Ecp2.
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:SF1; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR Pfam; PF14856; Hce2; 1.
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; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 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:UP000030104}.
FT DOMAIN 17..62
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 220..538
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1057 AA; 114245 MW; B6D60E8A0A3ECB39 CRC64;
MATTAVATKI RARAECRAVQ VDYGNGCPEL AAKCGISAAD FTKYNPASDF CSKLKPKQHV
CCSQGILPDF SPKPNADGSC YAYKVKDNDN CDDLAAEWSL TRQDLEDFNK NTWGWNGCTP
MYSKTVMCLS KGTAPFPAEI ANAQCGPQKP GSKPPTDGSD ISDLNPCPLN ACCNVWGQCG
ITRDFCIDTN TGPPGTAKEG TYGCISNCGM DVVKGSGSGA IQVAYYEGYN MKRDCLFQDA
SQIDTSKFTH VHFGFGTLTP SFDVETGDVL SSYNFGQFKK LYDVKRILSF GGWDFSTMPD
TYQIFRNGVK PANRLAMAQK IATFIKDNNL DGVDIDWEYP SATDLPENDP GSKEDGPNYL
AFLIVLKNLL PGKSVSIAAP ASYCQVNLTE TRQSLAMITK AGVPGNKVVV GVTSYGRSFK
MAEAGCYGPS CLYTGDRLNS NAKKGKCTGT AGYIADAEIA EILNNPKRSV TQHFVDSSSN
SDILVYDDTE YVSYMSAATK ATRAALYKAW GLGGTSDWAS DLQTYNEVPK PAKSWDAFFK
RVLDGEDPEV DDTRNGNWTE FNCDHEMTVH PTAYLPSPDY YDTLFHASVI ATTALDDLDN
KFAPIPPAKD NTWLLPLIDL LALGTLGTAG PFFNTVLNKL PYFLEKSSTL DNFKDTTMTM
VGQGTTIAKD LLPSDDPNSR WNPQSQDTFS NYMGQVVDGW ANVSSLSLEQ LFDGKPKSIK
TLGEIISNGK LVDGKFEQEP SKDDEATDIN DLRTNIQKCF FGYSIPALWQ ASKAYAFIID
AGYACGGKEP TDYLADDTMD ATGACVDGQQ YYLVYPDGDA TVCKRYCSDH GPCSQACSDN
KFSAPPGLDS LKGGNFGGIS KSDLVKGSVR TWKQNGKTNG GGYADPTDQD TINSLLNVDV
TTPGFMRIPV CSPERAYQSW DTAKAGSSDN YPCDIPPGRN TCGDSTFGNE TSDGSPLVED
CLTIIKNIQG DASTRYTTLV VGKNQREIAA HGTCAFGVQA TKVDGNANFV TGGQDVIDII
NESVKRFASN GKVGAKGNMN CNGNVKSEPV LWGIYST
//
