ID Q89YP1_BACTN Unreviewed; 481 AA.
AC Q89YP1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AAO79795.1};
GN OrderedLocusNames=BT_4690 {ECO:0000313|EMBL:AAO79795.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO79795.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO79795.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO79795.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; AE015928; AAO79795.1; -; Genomic_DNA.
DR RefSeq; NP_813601.1; NC_004663.1.
DR RefSeq; WP_011109383.1; NC_004663.1.
DR AlphaFoldDB; Q89YP1; -.
DR STRING; 226186.BT_4690; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 226186-BT_4690; -.
DR EnsemblBacteria; AAO79795; AAO79795; BT_4690.
DR GeneID; 60925862; -.
DR KEGG; bth:BT_4690; -.
DR PATRIC; fig|226186.12.peg.4769; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_024572_2_0_10; -.
DR InParanoid; Q89YP1; -.
DR OMA; FFHWYYP; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001414}.
FT DOMAIN 4..410
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; 55344 MW; B6BF237011F5EE1A CRC64;
MENGVMMQYF EWHLPNDGKL WKQIKEDALH LHDIGVTAVW IPPAYKADEQ QDEGYATYDL
YDLGEFDQKG TIRTKYGTKD ELKKMIDELH KYHIAVYLDV VLNHKAGGDF TEKFMVVEVD
PKERTKALGE PFEIQGWTGY SFHGRKDKHS DFKWHWYHFS GTGFDDAQKR SGVFQIQGEG
KAWSEGVDSE NGNYDFLLCN DIDLDHPEVV SELNRWGKWV SNELNLDGMR LDAIKHMKDQ
FVAQFLDAVR SERGNDFYAV GEYWNGDLEA LDAYIEAVGH KVNLFDVPLH YNMFQASQEG
KDYDLRDILK DTLVEHHPDL AVTIVDNHDT QRGSSLESNV EDWFKPLAYG LILLMKEGYP
CLFYGDYYGI KGEKSPHTRI IDILLDARRK YAYGDQIEYF DHPSTIGFIR TGDEEHNGSG
LVFLMSNDEA GSKIMSLGEK HKGEVWHEIT GSISEEITLD EEGNGEFSVE SRNLAVWVKK
D
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