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Database: UniProt
Entry: G3XMM4_ASPNA
LinkDB: G3XMM4_ASPNA
Original site: G3XMM4_ASPNA 
ID   G3XMM4_ASPNA            Unreviewed;       511 AA.
AC   G3XMM4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EHA28337.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:EHA28337.1};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_122069 {ECO:0000313|EMBL:EHA28337.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA28337.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA28337.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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:EHA28337.1}.
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DR   EMBL; ACJE01000001; EHA28337.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XMM4; -.
DR   STRING; 380704.G3XMM4; -.
DR   HOGENOM; CLU_024572_2_0_1; -.
DR   Proteomes; UP000009038; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 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   Glycosidase {ECO:0000313|EMBL:EHA28337.1};
KW   Hydrolase {ECO:0000313|EMBL:EHA28337.1}.
FT   DOMAIN          19..422
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHA28337.1"
FT   NON_TER         511
FT                   /evidence="ECO:0000313|EMBL:EHA28337.1"
SQ   SEQUENCE   511 AA;  57583 MW;  D9238D2AC5E69D97 CRC64;
     EKANAIESLP SWHSPTENTL LFQAFEWHVP ATPNTADKRS HWRRLQHALP AIHSLGVTSI
     WIPPGCKGMD AHGNGYDIYD LYDLGEFDQK GAVRTKWGTR GELEDLVRDA NALGVGVLWD
     AVLNHKAGAD SVERFEGVRV DDDRRDIEDG NPQQISGWTS FTFPGRGTTY SPLQYHWQHF
     SGVDWDDAQQ RKAIYKILDP SRPDKNWAQD VGTDENGNYD YLMFADLDFS HPEVREDVLR
     WGKWIMSVLP LSGMRLDAAK HFSTAFQREF IDCVRQEAGD RKVFVIGEYW SGELRALLRY
     LEEMEYRVAA VDVPLVERFS RLSRVKRADL RGVLRGTLVE SRPGNALQPG QMLETIVEPS
     FKPLAYALIL LRQGGHPCVF YGDLYGTCDG DHPPTPACEG QLPNLMRARK LYAYGEQQDY
     FDQPNCIGFI RYGNAAHPSG LACVMSNGGP ATKRMYVGRK HAGEKWTDLL QRGGDHPSVT
     VIDEMGYGEF PVQSMRVSVW VDSAADGREG V
//
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