ID   Q4X0H4_ASPFU            Unreviewed;       561 AA.
AC   Q4X0H4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=AFUA_2G13460 {ECO:0000313|EMBL:EAL93641.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL93641.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL93641.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:EAL93641.1}.
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DR   EMBL; AAHF01000001; EAL93641.1; -; Genomic_DNA.
DR   RefSeq; XP_755679.1; XM_750586.1.
DR   AlphaFoldDB; Q4X0H4; -.
DR   SMR; Q4X0H4; -.
DR   STRING; 330879.Q4X0H4; -.
DR   EnsemblFungi; EAL93641; EAL93641; AFUA_2G13460.
DR   GeneID; 3513769; -.
DR   KEGG; afm:AFUA_2G13460; -.
DR   VEuPathDB; FungiDB:Afu2g13460; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; Q4X0H4; -.
DR   OMA; HGYWIAD; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
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:SF208; 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, ECO:0000313|EMBL:EAL93641.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAL93641.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..561
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004245954"
FT   DOMAIN          35..394
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          504..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        257
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   SITE            322
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT   DISULFID        52..58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        177..191
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        267..308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        464..499
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ   SEQUENCE   561 AA;  61923 MW;  CA8C8A2280D7C48B CRC64;
     MRQSLYHGAI WFALASLASA DAPSSQQWAE RAIYQVMTDR FARPAGSSDA PCDPERYCGG
     SWTGIIDKLD YIQDLGFTAI QISPVVENIP DNTKYGEAYH GYWPKNLYAL NEHFGTADEL
     RRLVSEVHRR DMYLIVDVVI NDMAQAVNGS MKDDPSLKID YSQLFPFDDE KYYHPFCAIT
     DWTDPKIYKN CWFAVETVAL PDLNTGDASV ATMIGDWIKQ FVGNYSIDGL RIDAALHMDD
     DYVEGFSKAA GLFTIGEVSN GDTSLVCKYE NLVSSVLNYP LYYALIQAFT AGNMLGLAES
     IRAVQKDCKD FALLETFVEN HDLPRFASLT NDTTLAKNAM AFNILSDGIP QVYQGQEQHM
     SGNYTPFNRG ALWTTNYDTT SPLFKLTATL NKLRNHAISI DNHYVTNHSI ELHSDNSTYA
     TRKGPEGVQA VSVFSNQGTN GGKYQLALKD AYAPGTEVME VLGCSKLTTD DVGNLTVEMD
     AGEPRIFFPV AQLKNSGLCG FEKQKTASSS NSDRDSNSND STHPSSQDKD ADKKSSASIV
     GVPYPGMLIS GAALAFLSWF L
//