ID A0A074YX41_AURSE Unreviewed; 493 AA.
AC A0A074YX41;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=AUEXF2481DRAFT_45851 {ECO:0000313|EMBL:KEQ98737.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ98737.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ98737.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ98737.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584751; KEQ98737.1; -; Genomic_DNA.
DR RefSeq; XP_013347533.1; XM_013492079.1.
DR AlphaFoldDB; A0A074YX41; -.
DR STRING; 1043005.A0A074YX41; -.
DR GeneID; 25368015; -.
DR HOGENOM; CLU_006462_7_2_1; -.
DR InParanoid; A0A074YX41; -.
DR OMA; AHNWLFT; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000030641; 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:SF215; ALPHA-AMYLASE 1; 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, ECO:0000313|EMBL:KEQ98737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030641};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..493
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001704794"
FT DOMAIN 31..385
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 246
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 48..55
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 167..180
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 256..299
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 456..491
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 493 AA; 54784 MW; 91207A18A7131E18 CRC64;
MKLAVFFTLF TFGVSVLAAS AADWRSKSIY QVLTDRFARS DGSTTAKCDP VGKYCGGSYQ
GIIKELDYIQ NMGFTAIWIS PITFQLQTWT PYGEPWHGYW QQDLFKLNSA FGTAEDLRDL
ATALHNRGMY LMVDIVVNHN GWNGNASSVD YSVFQPFDNA EYYHNYCTVD YDNNTSIRDC
WLGDSNVELV DLRTEDTVVA QEYQTWIHQL VANYSIDGLR IDTVKHVDTD FWSGFGEAAG
VFITGEITNG DPYGLCPYQN YMDSVLNYAM YYAATAAFSS TSGSMSSFVS QLKGMKSQCK
DTTVLGSFSE NHDQPRFASL TDDISLAKSI ITYTIMSDGI PIMYEGQEQH YSGASDPYNR
EAVWLSGYNT GAPLYTHTAS TNQIRSHALY VDADWLTYKN WVIYSNSNNV AMRKGYDGYQ
TITVLTNNGA GSEDYTLSVT NTGYTNGMTV VDVLSCEVLS AGTDGTLAVP MSQGLPKIYY
PVELLDCSGI CGY
//
