ID   A0A0X8G3N7_9FIRM        Unreviewed;       554 AA.
AC   A0A0X8G3N7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=AT726_11665 {ECO:0000313|EMBL:AMC09496.1};
OS   Turicibacter sp. H121.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Turicibacteraceae; Turicibacter.
OX   NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC09496.1, ECO:0000313|Proteomes:UP000057144};
RN   [1] {ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMC09496.1, ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|EMBL:AMC09496.1,
RC   ECO:0000313|Proteomes:UP000057144};
RX   PubMed=27013036;
RA   Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA   Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT   "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT   the Feces of a Contaminated Germ-Free Mouse.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP013476; AMC09496.1; -; Genomic_DNA.
DR   RefSeq; WP_068759645.1; NZ_JAMQUX010000026.1.
DR   AlphaFoldDB; A0A0X8G3N7; -.
DR   STRING; 1712675.AT726_11665; -.
DR   KEGG; tur:AT726_11665; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000057144; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF178; OLIGO-1,6-GLUCOSIDASE 3-RELATED; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:AMC09496.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057144}.
FT   DOMAIN          13..415
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   554 AA;  64249 MW;  E06E9F414A1E9944 CRC64;
     MNKVWWKEAV AYQIYPRSFM DSNGDGIGDL NGIILKLDYL KALGIDVIWV SPFYKSPNDD
     CGYDISDYKD IMDEFGTMED FDRLLEEVHK RGMKLIADLV INHTSDEHPW FIESRSSVDH
     PKRDWYIWRD GVNGAEPNNW ESIFSGSAWE YDENTGQYYM HLFSKKQPDL NWENAEVREA
     LYEMVNWWLD KGIDGFRVDA ISHIKKEEGL TDMPNPHALK YVSSFDKHMN VEGIHPLLDD
     LKANTFDKYD IMTVGEANGV KIEDAHLWVG EEEGKFNMVF QFEHLGLWKD NGDQGTDVRQ
     LKKILTKWQK GLEGVGWNAL YIENHDLARI VSTLGDDQNY WKESATSLGM MYFMMKGTPF
     IYQGQEIGMT NVQFDKVEDY QDVQSTGLYY SKLEQGMSHE DIMEIIWATA RGNSRTPMQW
     NDGVNSGFTT GTPWLAVNPN YQTINVEAQE EDPDSILNFY KEMIALRKSE DIFVYGTYDL
     VFEDHQEIYA YTRTLGEKRV LILCNLTNKQ TSINLEKITV STDQLLLSNI PVEEHESIQE
     LTLKPFEARI YSLN
//