ID A0A2H3INC7_9EURO Unreviewed; 578 AA.
AC A0A2H3INC7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glycoside hydrolase, superfamily {ECO:0000313|EMBL:PCG94348.1};
GN ORFNames=PENO1_078930 {ECO:0000313|EMBL:PCG94348.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG94348.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG94348.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG94348.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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:PCG94348.1}.
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DR EMBL; NPFK01000282; PCG94348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3INC7; -.
DR STRING; 290292.A0A2H3INC7; -.
DR OrthoDB; 3680211at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF232; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:PCG94348.1};
KW Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 17..436
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 578 AA; 67549 MW; 079D4D05B11ECA20 CRC64;
MSPPVNRAWW KESSVYQIWP ASYKDSNNDG IGDIPGIISK LDYIKGLGMD IIWLSPSYKS
PQVDMGYDIS DYYSIHPPYG TVEDVDKLIS GCHERGMKLL MDLVVNHTSD QHEWFQKSRQ
SKDNEFRDWY IWKPPKFDER GNRHPPNNWV SHFQGSAWKY DTLTGEYYLH LYAEEQPDLN
WEHPPVRKAV HDIIRFWLDK GCDGFRMDVI NFISKNQEFP DGPVTNPDTP WQWGYTHYAN
GPRLHEYLQE IGQILQEYDA FSVGEMPFAT TIEDVLKAVR FDRKEINMIF DFEHVDIDHG
KLDKFGPGGW KLTDLKRMFN KWQTFMYQNE GWNALYWENH DQPRSIDRYT GASAEHSVIA
GKMLATCLAL MAGTPFVYQG QELGMRNVPV EWPIDEYQDI DCLNHWKRHL ETEHDNIEAL
TNYRKEYQKK SRDNARTPVQ WTAGPNAGFT DDANVKPWMS VNPNYRHINA ESQVSDPASV
YNYWRSVLGL RKKYLDIFVY GDFVLVDRDN ENLFAYTRQF EDQKALVVCN FTDRRVEWDS
VEILVGGEGK EVLLDNYGAS ERFKGGLRPY EAVVLLLA
//
