ID A0A1I5CY45_9FLAO Unreviewed; 482 AA.
AC A0A1I5CY45;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:SFN91551.1};
GN ORFNames=SAMN05660413_03066 {ECO:0000313|EMBL:SFN91551.1};
OS Salegentibacter flavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=287099 {ECO:0000313|EMBL:SFN91551.1, ECO:0000313|Proteomes:UP000199153};
RN [1] {ECO:0000313|EMBL:SFN91551.1, ECO:0000313|Proteomes:UP000199153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17794 {ECO:0000313|EMBL:SFN91551.1,
RC ECO:0000313|Proteomes:UP000199153};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; FOVL01000025; SFN91551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5CY45; -.
DR STRING; 287099.SAMN05660413_03066; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000199153; 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; cd11314; AmyAc_arch_bac_plant_AmyA; 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; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199153};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011493394"
FT DOMAIN 59..392
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 276
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 482 AA; 55427 MW; 7F8595E3748BBB52 CRC64;
MKKIKLILPV FLGLVLSFSS CSKDDDEIVD PGDDNSGEIP VEPNEPELLE LRNYSSGQKV
MMQTFYWDVE PRHEWWTTLS DKVEGWADAG IDRLWFPVAT KGQSGGYSMG YDPSDYFDFG
EYYQQQTTPT RFGTRTELEA LIEKSHNLGL EVIADIVINH NSGGGKEYNP YRDKDTWTLF
NEENGNASGW FNRNYENFYP NSTSPYDDGS LFYEETNLDH NQEYVQDWLW KKENSVAKYY
MNEMGFDGWR FDYVAGFEPW VVKAWLDEVG GFSVAELWDG NASNLANYVE ETGSGAFDFA
TFYKLDEAFD RHDDLTFLER DMLWKTHPDK AVTFTANHDT EKDDNEDNNI SVENKMKAYA
FILTHPGYPT IFYSDYENEN FQAEIQQLIE IHNSLAVGDI EILHVDKDEY IMKRNGNNEN
PGLIIYISTG ENTKRRNVQT NWKNVTLLDY SGNSTYIPTS DENGTASLEA PANGYAIWSV
SK
//
