ID E1WT49_BACF6 Unreviewed; 481 AA.
AC E1WT49;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
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};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 OMA; FFHWYYP; -.
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:SF7; ALPHA-AMYLASE 2-RELATED; 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 3: Inferred from homology;
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
//