ID   E1WT49_BACF6            Unreviewed;       481 AA.
AC   E1WT49;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Putative alpha-amylase {ECO:0000313|EMBL:CBW23549.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CBW23549.1};
GN   OrderedLocusNames=BF638R_3074 {ECO:0000313|EMBL:CBW23549.1};
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23549.1, ECO:0000313|Proteomes:UP000008560};
RN   [1] {ECO:0000313|EMBL:CBW23549.1, ECO:0000313|Proteomes:UP000008560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R {ECO:0000313|EMBL:CBW23549.1,
RC   ECO:0000313|Proteomes:UP000008560};
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; FQ312004; CBW23549.1; -; Genomic_DNA.
DR   RefSeq; WP_014299186.1; NC_016776.1.
DR   AlphaFoldDB; E1WT49; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; bfg:BF638R_3074; -.
DR   PATRIC; fig|862962.3.peg.3159; -.
DR   HOGENOM; CLU_024572_2_0_10; -.
DR   Proteomes; UP000008560; 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; IPR015237; Alpha-amylase_C_pro.
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; PF09154; Alpha-amy_C_pro; 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:CBW23549.1};
KW   Hydrolase {ECO:0000313|EMBL:CBW23549.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN          4..388
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        262
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         236
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   481 AA;  55327 MW;  A8CBA43DEED6B6E1 CRC64;
     MENGVMMQYF EWNLPNDGNL WKQLKEDASH LHEIGVTAVW IPPAYKADEQ QDEGYATYDL
     YDLGEFDQKG TVRTKYGTKE ELKEMIDELH KNHISVYLDV VLNHKAGGDF TEKFIVVEVD
     PNDRTQALGK PFEIQGWTGY SFHGRKDKYS DFKWHWYHFS GTGFNDAKKR SGIFQIQGEG
     KAWSEGVDNE NGNYDFLLCN DIDLDHPEVV TELNRWGKWV SKELNLDGMR LDAIKHMKDK
     FIAQFLDAVR SERGDKFYAV GEYWNGDLNT LDAYIKSVGH KVNLFDVPLH YNLFQASQEG
     KNYDLQNILK NTLVEHHCDL AVTFVDNHDS QSGSSLESQI EDWFKPLAYG LILLMKDGYP
     CLFYGDYYGV KGENSPHTQI INILLDTRRK YAYGDQIEYF DHPSAIGFIR TGDEEHVGSG
     LVFLMSNDEA GSKKMDLGEE HKGEIWHEIT GNIQQEITLD EKGSGEFSVN TRNIAVWIKK
     N
//