ID Q5LAX9_BACFN Unreviewed; 481 AA.
AC Q5LAX9; A0A380YPG4;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAH08743.1, ECO:0000313|EMBL:SUV36435.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:CAH08743.1, ECO:0000313|EMBL:SUV36435.1};
GN ORFNames=BF9343_2962 {ECO:0000313|EMBL:CAH08743.1}, NCTC9343_00252
GN {ECO:0000313|EMBL:SUV36435.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08743.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH08743.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
RN [2] {ECO:0000313|EMBL:SUV36435.1, ECO:0000313|Proteomes:UP000255401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9343 {ECO:0000313|EMBL:SUV36435.1,
RC ECO:0000313|Proteomes:UP000255401};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR626927; CAH08743.1; -; Genomic_DNA.
DR EMBL; UFTH01000001; SUV36435.1; -; Genomic_DNA.
DR RefSeq; WP_010993241.1; NZ_UFTH01000001.1.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 272559-BF9343_2962; -.
DR KEGG; bfs:BF9343_2962; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_024572_2_0_10; -.
DR OMA; FFHWYYP; -.
DR BioCyc; BFRA272559:G1GHZ-3215-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR Proteomes; UP000255401; Unassembled WGS sequence.
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:CAH08743.1};
KW Hydrolase {ECO:0000313|EMBL:CAH08743.1};
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; 55280 MW; 24C6A0A0ACEC6D4F CRC64;
MENGVMMQYF EWNLPNDGNL WKQLKEDASH LHEIGVTAVW IPPAYKADEQ QDEGYATYDL
YDLGEFDQKE TVRTKYGTKE ELKEMIDELH KNHISVYLDV VLNHKAGGDF TEKFIVVEVD
PNDRTQALGK PFEIQGWTGY SFHGRKDKYS DFKWHWYHFS GTGFDDAKKR SGIFQIQGEG
KAWSEGVDNE NGNYDFLLCN DIDLDHPEVV TELNRWGKWV SKELNLDGMR LDAIKHMKDK
FIAQFLDAVR SERGDKFYAV GEYWNGDLNT LDAYIKSVGH KVNLFDVPLH YNLFQASQEG
KNYDLQNILK NTLVGHHCDL AVTFVDNHDS QSGSSLESQI EDWFKPLAYG LILLIKDGYP
CLFYGDYYGV KGENSPHTQI INILLDARRK YAYGDQIEYF DHPSAIGFIR TGDEEHVGSG
LVFLMSNDEA GSKKMDLGEE HKGEIWHEIT GNIQQEITLD EKGSGEFSVN TRNIAVWIKK
N
//