ID S7Z6T2_PENO1 Unreviewed; 626 AA.
AC S7Z6T2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PDE_01201 {ECO:0000313|EMBL:EPS26265.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26265.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26265.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; KB644408; EPS26265.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z6T2; -.
DR SMR; S7Z6T2; -.
DR STRING; 933388.S7Z6T2; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OrthoDB; 3249969at2759; -.
DR PhylomeDB; S7Z6T2; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF00686; CBM_20; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..626
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004559733"
FT DOMAIN 518..626
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 626 AA; 67562 MW; 124A55521361E50B CRC64;
MKFLGLAALF LAQTVAGLTA AQWRSQSIYF LMTDRFGRTD NSVTASCNTN DRVYCGGTWQ
GIINQLDYIQ GMGFTAIWIT PVTEQLPQDT GDGEAYHGYW QQEIYNVNNN YGTAADLKAL
SQALHSRGMY LMVDVVANHM GYAGAGNTVD YSVFKPFSSS SYFHPYCLIS DYSNQTNVED
CWLGDTTVSL PDLDTTLSSV QTIWYNWVSD LVSNYSIDGL RIDTVKHVEK SFWPGYQSAA
GVYCVGEVFS GDPAYTCPYQ NYLDGVLNYP IYYQLLGAFK STSGSISSLY NMINSVASDC
ADPTLLGNFI ENHDNPRFAS YTSDYSQAKN VISFIFLSDG IPIVYAGQEQ HYSGGNDPAN
REATWLSGYS KNAQLYQHIA STNKIRSLAI SKDANYITSK NNAFYTDSNT IAMKKGSSGS
QVVTVLSNRG SSGSSYTLSL SGSGYEAGTK LVEMYTCTAV TVDSNGNIAV SMTSGLPRVF
MLASSACSLC SSACSLCSSA CSATATTLKT TTATATSCTQ ATALPVLFKD TVATSYGQSV
YLAGSISQLG SWNAANAVAL SADKYTSSNP LWYATVTLPV GTSFQYKFIK KTSSSGSVTW
ESDPNRSYTV PTGCVGSTAT VTATWR
//
