ID   D1AN48_SEBTE            Unreviewed;       481 AA.
AC   D1AN48;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:ACZ09652.1};
GN   OrderedLocusNames=Sterm_2808 {ECO:0000313|EMBL:ACZ09652.1};
OS   Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Sebaldella.
OX   NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ09652.1, ECO:0000313|Proteomes:UP000000845};
RN   [1] {ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA   Woyke T., Wu D., Eisen J.A.;
RT   "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ09652.1, ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX   PubMed=21304705;
RA   Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Chen F.;
RT   "Complete genome sequence of Sebaldella termitidis type strain
RT   (NCTC 11300).";
RL   Stand. Genomic Sci. 2:220-227(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP001739; ACZ09652.1; -; Genomic_DNA.
DR   RefSeq; WP_012862246.1; NC_013517.1.
DR   AlphaFoldDB; D1AN48; -.
DR   STRING; 526218.Sterm_2808; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; str:Sterm_2808; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_0; -.
DR   Proteomes; UP000000845; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000845}.
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         184
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         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;  55518 MW;  8C8A0FE733539B7C CRC64;
     MENGVMIQYF EWNLPADKKH WKRLADDAEH LKDIGINAVW IPPATKGTSD LDVGYGAYDL
     YDLGEFDQKG TVATKYGTKE ELITAIEALH EREISVYLDA VMNHKAGADE TERFMVQEVD
     PNDRNKAISD PYEIEGWTKF NFDGRNNKYS DFKWHWYHFN GTDYNNINQK TAIYKMTGDG
     KNWDQGVDDE NGNYDYLMFA NIDYERGDVV EEMKRWGVWV ANELNLDGFR LDAIKHINNN
     FIEEFLKEVR KVRGEDFYAV GEYWKGDLGS IVEYLDNVNY QADLFDVPLH FNFFTASKNG
     SAYDLREVFN NSLVINKKLF SVTFVDNHDS QWGSSLESQI DSWFKPLAYA LILLIADGYP
     CIFYGDYYGV GGKESPHRWV IEKLLYARKN YAYGEQINYF DDPNLIGMVR KGNEDHPGSG
     LVMLLSNHTE GTKKINIGKE HAGEVWYEIT ENIKDEIHID DNGEAEFKVN AGKAAVWVKK
     Q
//