ID A1CCW9_ASPCL Unreviewed; 544 AA.
AC A1CCW9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=ACLA_063440 {ECO:0000313|EMBL:EAW12376.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12376.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12376.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(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; DS027050; EAW12376.1; -; Genomic_DNA.
DR RefSeq; XP_001273802.1; XM_001273801.1.
DR AlphaFoldDB; A1CCW9; -.
DR SMR; A1CCW9; -.
DR STRING; 344612.A1CCW9; -.
DR EnsemblFungi; EAW12376; EAW12376; ACLA_063440.
DR GeneID; 4705957; -.
DR KEGG; act:ACLA_063440; -.
DR VEuPathDB; FungiDB:ACLA_063440; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OMA; NAQLCQT; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000006701; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 22..384
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 39..47
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 163..177
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 254..296
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 455..490
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 544 AA; 61167 MW; 0BBE4527DB89754C CRC64;
MFAHPSTWAA NTSQWKPRAI YQTMTDRFAR TDGSTTAHCV SSERIYCGGT WRGMINQLDY
IQGMGFDAVM ISPVIKNVEG RVEYGEAYHG YWPIDLYELN PHFGTEQDLL DLSAAVHKRG
MFLMMDTIIN NMAYITNGSD PATSIDYSVF KPFNSESYFH KYCKITNWLD PQNYQTCQTG
DNIVPLPDLF TEHDEVQQTL IKWAQDMIAK YSIDGLRIDA AKHVNTGFLY NFGKALGDTF
MTGEVYDSSV DMICDYKNHY ITSVPNFPIF YAVIDVFTQS KMEELPNAIE VMKHSCQDTN
GLTLFTESHD VSRFANRTDD IVLAKNVVTF NILFDGIPII YQGQEQHFHG SYEDQNSNRE
AVWLSGYNRD AVLYKHIRTM NRIRKHAYNL DPDWFNMQTI PIYQGESELA FRKGIEGRQM
VMVLSAQGTK QTGQYDLALP VSYNPGVVAM DVISCVNYTA NDVGQITINM KTADPQVLFP
ADLMAGSGLC GYSESNISYV ELKTGRKSPT VSSPSAGVAV APVRSMSVTI LFSLLMSIAI
AVLS
//