ID A0A2R7KTP0_9SPHI Unreviewed; 496 AA.
AC A0A2R7KTP0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:PTT00767.1};
GN ORFNames=DBR11_09095 {ECO:0000313|EMBL:PTT00767.1};
OS Pedobacter sp. HMWF019.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2056856 {ECO:0000313|EMBL:PTT00767.1, ECO:0000313|Proteomes:UP000244301};
RN [1] {ECO:0000313|EMBL:PTT00767.1, ECO:0000313|Proteomes:UP000244301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMWF019 {ECO:0000313|EMBL:PTT00767.1,
RC ECO:0000313|Proteomes:UP000244301};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PTT00767.1}.
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DR EMBL; QAIL01000141; PTT00767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R7KTP0; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000244301; 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; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000244301}.
FT DOMAIN 4..393
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 104
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 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 496 AA; 57158 MW; 0D99B8A330A4F4E6 CRC64;
MTNQLLIQYF HWYYNENEQL WEKTAREARN LSALGVTGAW LPPAYKATSG GYSVGYDCYD
LFDLGEFDQK GSIPTKYGTK ETYLKAVKAL NDAGVSTIAD MVFNHKAGAD ELETIKVRKV
DPDNRLEFIS DVMDIEAWTK FTFPGRKGLY SDFVWDHQCF SGIDRSENPP EDGIFSIQNE
YGEGWEEVPS TEYGNYDYLM FNDIEFRNPA VREELKRWGE WYYETCGMDG FRLDAVKHIS
ADFLNEWLDH MKSTFKREFF VVAENWIIEG VEELDAYLQR TDGRMQLFDS ILHHNLYLAG
KEGEDYDLSK IFEGTLVAYH PELSVTFVDN HDSQPLQALE SYVDFWFRPM AYALILLREQ
GIPCLFYPDL YGCKYTDKNE EGEDVEVELV ALEELPLLCQ IRKERAFGVQ RDYLDYPSCI
GWTREGVDEM PGSGFAVVMS NSNEGFKDME IGTRHAGQVF IDALGRMAEE VVINEEGWAQ
FACIAGNISV WILKED
//
