ID   I7LW22_TETTS            Unreviewed;       486 AA.
AC   I7LW22;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=TTHERM_00411610 {ECO:0000313|EMBL:EAS00610.1};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS00610.1, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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};
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DR   EMBL; GG662612; EAS00610.1; -; Genomic_DNA.
DR   RefSeq; XP_001020855.1; XM_001020855.3.
DR   AlphaFoldDB; I7LW22; -.
DR   STRING; 312017.I7LW22; -.
DR   EnsemblProtists; EAS00610; EAS00610; TTHERM_00411610.
DR   GeneID; 7825464; -.
DR   KEGG; tet:TTHERM_00411610; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; I7LW22; -.
DR   OMA; AHNWLFT; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11319; AmyAc_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 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.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..486
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003711837"
FT   DOMAIN          32..385
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        215
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        239
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   SITE            305
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
SQ   SEQUENCE   486 AA;  55363 MW;  21A4771D8D27C583 CRC64;
     MSKLQFVLIA ALLLVAVSAK TAQEWKTRNI YQIITDRFAL GDGSKPYCDL NKQPYYCGGN
     FKGIENNLDY IQGMGFNAIW ISPVPDNYPN QFHGYAAKNM TEINSHFGGA DGLKSLIDAC
     HKRDIWVMID VVANHMGNTD QNYSENIPFN SPDHYHSYCI ISDSDFATKN MYNIQHCRLA
     GLADLNQENS YVSNYLVNWI KDLVQTYNVD GIRIDTVPEV HPDFWKQYTT SAGVFATGEV
     FDGDFGYVAS YIPSVGSVLN YPWYFNMRDI FVNQKDMWGV RTYYQNWANQ HADLSILTPF
     VDNHDNPRFL SDQVFNNGKD RNTRIQLLKG YTTFTLTSIG IPILYYGTEQ YFSGNTDPYD
     REPLWNSLNT NSDMYKYVQS ILYAKNITNA GLQGQTEAYC DQDLYAFFRG KLFVGVTSKF
     NQVTRQIVTH PFSNGEVICN IFYPTQDCLT ITNNSFNLVL IGGEAKIFVP KSLLQKSSQF
     LRSASS
//