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Database: UniProt
Entry: A0A1Y2J3F4_PYCCO
LinkDB: A0A1Y2J3F4_PYCCO
Original site: A0A1Y2J3F4_PYCCO 
ID   A0A1Y2J3F4_PYCCO        Unreviewed;       577 AA.
AC   A0A1Y2J3F4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   ORFNames=PYCCODRAFT_1497577 {ECO:0000313|EMBL:OSD07916.1};
OS   Trametes coccinea BRFM310.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=1353009 {ECO:0000313|EMBL:OSD07916.1, ECO:0000313|Proteomes:UP000193067};
RN   [1] {ECO:0000313|EMBL:OSD07916.1, ECO:0000313|Proteomes:UP000193067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM310 {ECO:0000313|EMBL:OSD07916.1,
RC   ECO:0000313|Proteomes:UP000193067};
RX   PubMed=26692083; DOI=10.1186/s13068-015-0407-8;
RA   Couturier M., Navarro D., Chevret D., Henrissat B., Piumi F.,
RA   Ruiz-Duenas F.J., Martinez A.T., Grigoriev I.V., Riley R., Lipzen A.,
RA   Berrin J.G., Master E.R., Rosso M.N.;
RT   "Enhanced degradation of softwood versus hardwood by the white-rot fungus
RT   Pycnoporus coccineus.";
RL   Biotechnol. Biofuels 8:216-216(2015).
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         ECO:0000256|RuleBase:RU361134};
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, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; KZ084087; OSD07916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2J3F4; -.
DR   STRING; 1353009.A0A1Y2J3F4; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000193067; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   CDD; cd05808; CBM20_alpha_amylase; 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; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
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; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193067};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..577
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013050688"
FT   DOMAIN          477..577
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          554..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  61076 MW;  F83435183B03428F CRC64;
     MVLWISVGAW AAFYALSSTV HARPSDVVTP RSSLNSRAPT GNKDVIIQMF EWTWDSVAAE
     CTNFIGPAGY GFVQVSPPQE HIQGDQWWTD YQPVSYILTS KRGDRTQFAN MISTCHAAGV
     GVIADTIFNH MAGVDSGTGV AGSSFTHYNY PGIYQNQDFH HCGLEPGDDI VNYDNAVEVQ
     TCELDNLADL ATETEYVRSR LAEYANDLLS LGVDGLRLDA AKHINVTDIA NILSRLDRTV
     YITQEVIYGA GEPITPNQYT GNGNAFLGGG ISSLQSFDNL GWVPGTGANV FVTNHDTERN
     GNSLNDNSPS NTYVTAMIFS LAHPYGTPTI LSSYSGFTNT DAGAPNGGTG TCSGSGGENG
     WLCQHRWTAV AGMVGFRNNV GSAAMTNWVA PQSQQIAFGR GSLGFVAINN ADADWSTTFE
     TSLPDGSYCD VVSGTSSDGS CTGSSFNVSS GSLTATVPAR SAIAVHTGAK GTGNGSGSNS
     GSVTVNFAET ATTTFGENIF VVGSIPQLGN WDPASAIALS AASYPVWTVS VSIPAGTTFE
     YKFIRKETDG SIVWESDPNR EDTTPSSGSQ TINTSWR
//
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