ID J7TFG7_STRSL Unreviewed; 483 AA.
AC J7TFG7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EJO15506.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:EJO15506.1};
GN ORFNames=RSSL_00417 {ECO:0000313|EMBL:EJO15506.1};
OS Streptococcus salivarius K12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1200793 {ECO:0000313|EMBL:EJO15506.1, ECO:0000313|Proteomes:UP000006983};
RN [1] {ECO:0000313|EMBL:EJO15506.1, ECO:0000313|Proteomes:UP000006983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptococcus salivarius K12
RC {ECO:0000313|Proteomes:UP000006983};
RX PubMed=23045482; DOI=10.1128/JB.01268-12;
RA Barretto C., Alvarez-Martin P., Foata F., Renault P., Berger B.;
RT "Genome Sequence of the Lantibiotic Bacteriocin Producer Streptococcus
RT salivarius Strain K12.";
RL J. Bacteriol. 194:5959-5960(2012).
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:EJO15506.1}.
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DR EMBL; ALIF01000006; EJO15506.1; -; Genomic_DNA.
DR RefSeq; WP_002891527.1; NZ_ALIF01000006.1.
DR AlphaFoldDB; J7TFG7; -.
DR SMR; J7TFG7; -.
DR PATRIC; fig|1200793.3.peg.1497; -.
DR Proteomes; UP000006983; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
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: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 Glycosidase {ECO:0000313|EMBL:EJO15506.1};
KW Hydrolase {ECO:0000313|EMBL:EJO15506.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT DOMAIN 4..392
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 264
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 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 483 AA; 55489 MW; A2E97421DFC51D7C CRC64;
MTNQTAMQYF EWYLPSDGQH WNNLAEDAQH LADLGISHVW MPPAFKATNK DDVGYGVYDL
FDLGEFDQKG TVRTKYGLKE EYLNAINQLK EVGIVPMADV VLNHKAAADK LETFEVVEVD
PEDRTQEISE PFEIEGWTHF TFDGRNKAYD GFEWHWYHFN GTDFDAKRNK SGIYLIQGDN
KGWADNDLVD NENGNFDYLM YANLDYKHPE VIENIYEWAD WFVETTGVQG FRMDAVKHID
SFFMRNFIRD VKEKQGQDFY VFGEFWNGNE EDNNTYLEKI EKRFDLVDVS LHNNLHNAST
AGADYDLTTI FDHSLVKNHP EHAVTFVDNH DTQRGQALES TVEEWFKPAA YALILLREDG
LPCLFYGDYY GIEGEFAQEN FQESLDTLLY ARKDLAYGEQ TDYFDDPNCI GWTRSGNEDG
APLAVTISND AANSKSMEIG SDWAGQAFYD ILGNCSDTVT IDEDGWGDFP VSEKSVSVWT
IQD
//
