ID   D4JFK5_9FIRM            Unreviewed;       483 AA.
AC   D4JFK5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Glycosidases {ECO:0000313|EMBL:CBK88977.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CBK88977.1};
GN   ORFNames=EC1_16740 {ECO:0000313|EMBL:CBK88977.1};
OS   Faecalitalea cylindroides T2-87.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalitalea.
OX   NCBI_TaxID=717960 {ECO:0000313|EMBL:CBK88977.1, ECO:0000313|Proteomes:UP000008801};
RN   [1] {ECO:0000313|EMBL:CBK88977.1, ECO:0000313|Proteomes:UP000008801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2-87 {ECO:0000313|EMBL:CBK88977.1,
RC   ECO:0000313|Proteomes:UP000008801};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Eubacterium cylindroides T2-87.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK88977.1, ECO:0000313|Proteomes:UP000008801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2-87 {ECO:0000313|EMBL:CBK88977.1,
RC   ECO:0000313|Proteomes:UP000008801};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; FP929041; CBK88977.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JFK5; -.
DR   STRING; 717960.EC1_16740; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; euc:EC1_16740; -.
DR   PATRIC; fig|717960.3.peg.1162; -.
DR   HOGENOM; CLU_024572_2_1_9; -.
DR   Proteomes; UP000008801; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Glycosidase {ECO:0000313|EMBL:CBK88977.1};
KW   Hydrolase {ECO:0000313|EMBL:CBK88977.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN          4..387
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        261
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   483 AA;  56411 MW;  7472D3A4172FA6CD CRC64;
     MTKRTMIQYF EWYLKSDPPL YQTLMKEASS LSKMGFTHVW LPPAYKGQAG INDVGYGVYD
     MYDLGEFDQK GSIRTKYGTK DEYIQAIDVC HQNSLQVIAD IVFNHRMGAD EKETIKATAM
     DWNDRNRAVG QEKIVDVWTK YTFPVRNGKY SKFQWTWKDF DGTDYDAKTN QNVLMTFENK
     KWDPKVSKEE GNFDFIMGDD LDFQNPNVIE ELYHWGKWYK EFTNIDGYRL DAIKSIDSNF
     FKGWLDKQKS YHTNDVYAVG EYWSGDLNEL NTYLNDSGHC MHLFDVPLHF NLFNASSSYD
     TYDMSRILDH TLVSSQNEYA CPFVDNHDTQ PGQALYSWVQ GWFKLHAYSL ILLRNFDNPC
     VFYGDLYGIE HDNIGPVTHL SELVWIRSRI LEDEIEDRFD DFHCIGWKVD GKHPIVVVMT
     NGLANGKEFV IKNKSNIEFI DLVTKKTIKL DENGRGKFDC FDGGCSIFIE SEVYQKMKEE
     LEL
//