ID K9GR16_PEND1 Unreviewed; 510 AA.
AC K9GR16;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PDIP_40140 {ECO:0000313|EMBL:EKV15561.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV15561.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV15561.1}.
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DR EMBL; AKCU01000271; EKV15561.1; -; Genomic_DNA.
DR RefSeq; XP_014535005.1; XM_014679519.1.
DR AlphaFoldDB; K9GR16; -.
DR GeneID; 26232332; -.
DR KEGG; pdp:PDIP_40140; -.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000009886; 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:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF220; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 1..358
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 286
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 16..24
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 140..154
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 428..463
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 510 AA; 56629 MW; D20208C06685219F CRC64;
MTDRFARTDG STTAPCNTTA GLYCGGTWRG TMNQLDYIQG MGFDAVMISP ISENVHGQVY
YGEAYHGYWP VNLYNINSHF GTHQDLLDLS AAVHSRGMYL MLDTVINNMA YISNGSNPAT
SIDYSVFTPF NNADYFHPYC KITQWENMTN AQLCQTGDNY VPLPDLYTEH ADVQQLMIKW
ANNVIKTYSI DGLRIDAAKH VNPGFLENFR KGVDTFMTGE VLEGAVDIMV DYQTNYIDSL
PNYPIYFQIL AAFTDGHTSL LAQEVEKMRI SMPDVNAMAS FSENHDKPRI GSFSKDMAMA
KNILVFTMLF DGIPIIYQGQ EQHLSGNSVP VNREAIWHTK YDTSTELYQL IAKLNRIRNH
AAHLSADYFE DSTHPIFQGG SELAFTKGVQ GRQVVMVLST QSSTSGAYQI DMPVSYNAGT
VVMNVLSCKN YTVDNQGMLH VDMDKGEPRV FYPAQYMDGI GLCGYPDSNV SLTTLKTQNE
KTSAGVQSTS GTGLAALLLA VVSSIFVTFL
//
