ID   Q2LV73_SYNAS            Unreviewed;       531 AA.
AC   Q2LV73;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=SYN_00687 {ECO:0000313|EMBL:ABC77981.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77981.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC77981.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC77981.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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   -!- 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, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP000252; ABC77981.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LV73; -.
DR   STRING; 56780.SYN_00687; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; sat:SYN_00687; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_7_3_7; -.
DR   InParanoid; Q2LV73; -.
DR   Proteomes; UP000001933; 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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:ABC77981.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:ABC77981.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT   DOMAIN          38..428
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   531 AA;  61722 MW;  5B25DD57EC1752C8 CRC64;
     MIPASAMPLT QNIYKNLKPR INQPEEIMAI TRKDIIYFII TDRFYGIENQ KPEVKQKINK
     DNPFFYHGGN FDGIIEKIPY LKNLGITALW ITPVYRQIDL ETAHGYHGYW ALDFNAVNPV
     LYIDNGHYLP GSKYYLRDLV DRLHMNGIKL ILDVVVNHTG YRHPGIFDSL DNPTPICSSW
     FNRMNISLET SETEGQLSGL PDMDLDLPDV CDYHTETILS WLRETGVDGI RMDTVKHVER
     NFWTYFKTQV KGQFPGVTLL GEVLVFDIDN LSQYQKYDAI DQLFDFPMQN AIKNVFVYDH
     GMTDFISPYN IGTGILERDR SYSNHNQLVT LLDNHDLSAR FMTWILDRQA GDYRKATDVM
     KLTLTFLFTI RGIPQIYYGT ELGLEGHSDP DNRRDFPWEK LNADYEVKTE YSHEKEIYDH
     TRKMISIRRS NDALSSGYFV CLYVDYFLMI FLRYVEDNIV IAGFHNGWLD MPSEVIIDIG
     HNPDLPRRIR EKLSDATLVS LLDNQLHPIR EGKLKIRLGK KSAIILTIKN Q
//