ID   B6H6W6_PENRW            Unreviewed;       623 AA.
AC   B6H6W6;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=Pc16g00630 {ECO:0000313|EMBL:CAP92733.1}, PCH_Pc16g00630
GN   {ECO:0000313|EMBL:CAP92733.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92733.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92733.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP92733.1; -; Genomic_DNA.
DR   RefSeq; XP_002560482.1; XM_002560436.1.
DR   AlphaFoldDB; B6H6W6; -.
DR   STRING; 500485.B6H6W6; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 8317641; -.
DR   KEGG; pcs:Pc16g00630; -.
DR   VEuPathDB; FungiDB:PCH_Pc16g00630; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   OMA; YMDGVLN; -.
DR   OrthoDB; 3249969at2759; -.
DR   BioCyc; PCHR:PC16G00630-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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:UP000000724};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..623
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002845460"
FT   DOMAIN          515..623
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   623 AA;  67539 MW;  6A2F3DC18FA47664 CRC64;
     MKKVIFTATI LLWQMVMGLT PAEWRSQSIY FLLTDRFGRT DNSVTANCNV DDRAYCGGTW
     QGIINQLDYI QGMGFTAIWI TPVTKQLPQD TGYGMAYHGY WQQDIYDVND HHGTSDDLLA
     LSKALHARGM YLMVDVVANH MGYAGAGNTV DYSVFTPFSS SSYFHPYCLI SNYNDQSNVE
     NCWLGDTTVS LPDLDTTQNS VQTIWNDWIA DLVTKYSIDG LRIDTVKHVQ KSFWPGFNDA
     AGVYAVGEIF DGNPAYTCDY QNYMDGVLNY PIYYPLLRAF QSSSGSISDL YNMVGTVASS
     CADSTLLGNF IENHDNPRFP SYTSDYSQAK NVISFLFLSD GIPIVYAGQE QHYSGGHDPA
     NREAVWLSGY STTAELYQHI ATTNKIRKAA VAADSSYITS KNVPFYQDSH TLAMKKGSGS
     SPVITVLSNA GSSGSSYTLY LGGSGYSSGT KLMEMHTCTS ITVDSSGKIA VPMVSGLPRV
     LIPASSVSNS GLCGSSVPSA TATQTTTATT TGAGCTQATA LPVLFKELVT TVYGQDIYIS
     GSISQLGNWD TSQAIALSSS SYTASNPLWQ TTITLPVGTT FQYKFLKKTT GSSTVTWESD
     PNRSYTVPTG CTGATATVAA SWK
//