ID A0A135LRZ0_PENPA Unreviewed; 624 AA.
AC A0A135LRZ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PGRI_091050 {ECO:0000313|EMBL:KXG51712.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG51712.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG51712.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG51712.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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}.
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:KXG51712.1}.
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DR EMBL; LHQR01000029; KXG51712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LRZ0; -.
DR STRING; 5078.A0A135LRZ0; -.
DR OMA; YMDGVLN; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000070168; 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 Hydrolase {ECO:0000313|EMBL:KXG51712.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..624
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007800758"
FT DOMAIN 518..624
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 624 AA; 68057 MW; 8B4C862A08FFC462 CRC64;
MKRLIFTATI LLWQMVMGLT PAEWRSQSIY FLLTDRFGRS DNSVTANCNV NDRIYCGGTW
QGIINQLDYI QGMGFTAIWI TPVTKQLSQN TRDGSSYHGY WQQDIYNVNE NHGTSDDLLA
LSKALHARGM YLMVDVVANH MGYAGAGNNV DYSVFTPFNS ASYFHPYCMI SNYNDQSNVE
NCWLGDTIVS LPDLDTTKSS VQTLWNNWIS DLVSKYSIDG LRVDTVKHVQ KSFWPSFNKA
AGVYSVGEIF DGNPAYTCDY QKYMDGVLNY PMYYPLLRAF QSSSGSISDL YNMIGTVAST
CADSTLLGNF IENHDNPRFP SYTSDYSQAK NVLSFLFLSD GIPIVYSGQE QHYGGGNDPA
NREAIWLSKY STTAELYKYI ATTNKIRKAA IAADSSYITS KNVPFYQDSN TLAMKKGSGS
SPVITVLSNA GSSGSSYTLY LGGSGYSSGT KLMELYTCTS ITVDSSNKIA VPMASGLPRV
FILASSLGNS GLCGSTVPTT TATTATQTTT TTTTGTGCTQ ATALPVLFKE LVTTTFGQDI
YISGSISQLG SWDTSKAIAL SSGSYTSSNP LWQTTITLPV GTTFQYKFLK KTNGAVTWES
DPNRSYTVPT GCSGSTATVT ASWK
//
