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Database: UniProt
Entry: A0A2T4BLT5_9HYPO
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Original site: A0A2T4BLT5_9HYPO 
ID   A0A2T4BLT5_9HYPO        Unreviewed;       463 AA.
AC   A0A2T4BLT5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=BBK36DRAFT_1136951 {ECO:0000313|EMBL:PTB70277.1};
OS   Trichoderma citrinoviride.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB70277.1, ECO:0000313|Proteomes:UP000241546};
RN   [1] {ECO:0000313|Proteomes:UP000241546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG   DOE Joint Genome Institute;
RA   Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA   Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA   Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ680207; PTB70277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4BLT5; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000241546; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
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   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241546};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..463
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015487257"
FT   DOMAIN          32..372
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         238
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        159..172
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ   SEQUENCE   463 AA;  50493 MW;  42CC4C4F15DE5B97 CRC64;
     MKLRFALPLL LQLSLPVLSA DTAAWRSRTI YFALTDRIAR NSGDTGGSAC GNLGDYCGGT
     FQGLESKLDY IKGMGFDAIW ITPVVTNSDG GYHGYWAEDI DSINSHYGSA DDLKSLVNAA
     HSKGFYMMVD VVANHMGYAN ITDDSPTPLN QASSYHPECD IDYNNQTSVQ ECWISGLPDL
     DTESPTIRSL YQDWVSNLVS TYGFDGVRID TVKHVEQDYW PGFVNATGVY CIGEVFDGDP
     NYMLPYASLM PGLLNYAIYY PMTRFFLQQG SSQDMVNMHD QIGSMFPDPT ALGTFVDNHD
     NPRFLSTKND TALLKNALTY TILGRGIPIV YYGTEQAFSG GNDPANREDL WRSGFNTQSD
     MYDAISKLTY AKHAVGGLAD NDHTHLYVAD TAYAFSRAGG KMVALTTNSG SGSSAQHCFG
     TQVPNGSWQN VFDAGNGPTY TADGNGQLCL NVSNGQPIVL LSS
//
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