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Database: UniProt
Entry: A0A1Y4SY04_9FIRM
LinkDB: A0A1Y4SY04_9FIRM
Original site: A0A1Y4SY04_9FIRM 
ID   A0A1Y4SY04_9FIRM        Unreviewed;       478 AA.
AC   A0A1Y4SY04;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:OUQ33832.1};
GN   ORFNames=B5E75_08980 {ECO:0000313|EMBL:OUQ33832.1};
OS   Massilimicrobiota timonensis.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Massilimicrobiota.
OX   NCBI_TaxID=1776392 {ECO:0000313|EMBL:OUQ33832.1, ECO:0000313|Proteomes:UP000195305};
RN   [1] {ECO:0000313|Proteomes:UP000195305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An13 {ECO:0000313|Proteomes:UP000195305};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUQ33832.1}.
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DR   EMBL; NFLJ01000024; OUQ33832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4SY04; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000195305; Unassembled WGS sequence.
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; 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:SF49; ALPHA-AMYLASE; 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   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
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        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        261
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         235
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         300
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   478 AA;  56432 MW;  944FB5068418AE76 CRC64;
     MKQGVLMQYF EWYLPSQPFL FQKIQEDAKH LHDIGITALW LPPAYKGMAG SNDVGYGVYD
     LYDLGEFDQK GSIPTKYGTR EDYLKAIQTL HQYHIQVYGD IVFNHKMGAD GYEDVKASEV
     NQRNRYDVEV QEEWIRVPTL FTFPQRHQKY SDFTWDWTCF DGIDYDAKTK RHATFLFQDK
     NWDTQVDDEN GNYDYLMGAD LDFSNPRVVE ELERWGKWYW DTTHLDGFRL DAVKHIRASF
     FCHWLDCMRQ YTHQELFTVG EYWHGDVQKL LHYLKQVGGR MSLFDVPLHY HFYEASHSFG
     EYDMSKIFEG TLVQKACMNA VTFVDNHDTQ PQQGLQSWVM DWFKPLAYAL ILLRKDGYPC
     VFYGDYYGIA KPVIRGQSEI LDKLLYLRKH YAYGQQNDYF YDRHIIGWTR EMYGLACVMT
     NQKGGSLKMY VGTSYCHQIF YDYLGHHQQR VEIDEQGYGV FPVNDGSVSV YIMQKSGD
//
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