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Database: UniProt/TrEMBL
Entry: Q89YP1_BACTN
LinkDB: Q89YP1_BACTN
Original site: Q89YP1_BACTN 
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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