ID T0TJ14_9STRE Unreviewed; 483 AA.
AC T0TJ14;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cytoplasmic alpha-amylase {ECO:0000313|EMBL:EQC73440.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:EQC73440.1};
GN ORFNames=HSISS3_572 {ECO:0000313|EMBL:EQC73440.1};
OS Streptococcus sp. HSISS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1316412 {ECO:0000313|EMBL:EQC73440.1};
RN [1] {ECO:0000313|EMBL:EQC73440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSISS3 {ECO:0000313|EMBL:EQC73440.1};
RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA Kleerebezem M.;
RT "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL PLoS ONE 8:E83418-E83418(2013).
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:EQC73440.1}.
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DR EMBL; ASKH01000051; EQC73440.1; -; Genomic_DNA.
DR AlphaFoldDB; T0TJ14; -.
DR PATRIC; fig|1316412.3.peg.1501; -.
DR HOGENOM; CLU_024572_2_0_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000015931; Chromosome.
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:EQC73440.1};
KW Hydrolase {ECO:0000313|EMBL:EQC73440.1};
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; 55876 MW; CB1840F2C78BAF06 CRC64;
MTNQTVMQYF EWYLPSDGQH WNHLAEDAQH LSDLGISHVW MPPAFKGTNK DDVGYGVYDL
FDLGEFDQKG TIRTKYGFKD EYLNAINRLK DVGIVPMADV VLNHKAAADK LETFEVVEVD
PEDRTKEISK PFEIEGWTHF TFDGRQKAYN DFEWHWYHFN GTDFDAKRNK SGIYLIQGDN
KGWAENDLVD NENGNFDYLM YANLDYKHPE VIENIYSWVD WFVQTTGVLG FRMDAVKHID
SFFMRNFIRD VKEKQGQDFY VFGEFWNAKE EDNNTYLEKT ENRFDLVDVR LHNNLYDASL
EGADYDLTTI FDQTLVKNHP EHAVTFVENH DTQRGQALES TVEEWFKPAA YALILLREDG
LPCLFYGDYY GIEGEFAQES FQEVLDTLLY ARKELAYGEQ KDYFDDPNCI GWTRSGNEGG
TPLAVTISND VANSKTMEIG SDWAGQTFHD ILGNCSDTVT IDEDGWGDFP VSEKSVSVWT
IQD
//
