ID B5BQC3_HYPRU Unreviewed; 463 AA.
AC B5BQC3;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN Name=TRa2 {ECO:0000313|EMBL:BAG69580.1};
OS Hypocrea rufa (Trichoderma viride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5547 {ECO:0000313|EMBL:BAG69580.1};
RN [1] {ECO:0000313|EMBL:BAG69580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IAM 5141 {ECO:0000313|EMBL:BAG69580.1};
RA Noguchi A., Inohara-Ochiai M., Ishibashi N., Fukami H., Nakayama T.,
RA Nakao M.;
RT "A Novel Glucosylation Enzyme: Molecular Cloning, Expression, and
RT Characterization of Trichoderma viride JCM22452 alpha-Amylase and Enzymatic
RT Synthesis of Some Flavonoid Monoglucosides and Oligoglucosides.";
RL J. Agric. Food Chem. 56:12016-12024(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 ECO:0000256|RuleBase:RU361134};
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, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AB375856; BAG69580.1; -; mRNA.
DR AlphaFoldDB; B5BQC3; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CLAE; AMY13B_TRIVI; -.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF212; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|PIRSR:PIRSR001024-3};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001024-3};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..463
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002828706"
FT DOMAIN 33..372
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 300
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 160..173
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 463 AA; 50620 MW; 585A66687E415A8A CRC64;
MKLRSAVPLL LQLSLPAVLG ADTADWRSRT IYFALTDRIA RSSSDTGGSA CTNLNDYCGG
TFQGLESKLD YIKGMGFDAI WINPVVTNSD FGFHGYWALD LNTINSHYGT ADDLKSLVDA
AHGKGFYMMV DVVANHMGNA NITDDSPSPL NQQSSYHTKC DIDFNNQTSV ENCWLAGLPD
VDTQDPTIRS LYQDWVSNLV STYGFDGVRI DTVRHVEQDY WPGFVNASGV YCIGEVFNGD
PDFMQPYQSL MPGLLNYAIF YPLNAFYQQT GSSQALVDMH DRLSSFPDPT ALGTFVDNHD
NPRFLSVKND TSLFKNALTY TILGRGIPIV YYGSEQAFSG SNDPANREDL WRSGYNTETD
MYNAISKLTF AKHTAGGLAD NDHKHLYVEP TAYAWSRAGG KLVAFTTNSG GGSSAQFCFG
TQVPNGSWTN VFDGGNGPTY TADGNGQLCL TTTNGEPIVL LSS
//
