ID A0A0C2SG87_9BACL Unreviewed; 485 AA.
AC A0A0C2SG87;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:KIL52949.1};
GN ORFNames=KR50_02780 {ECO:0000313|EMBL:KIL52949.1};
OS Jeotgalibacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL52949.1, ECO:0000313|Proteomes:UP000031972};
RN [1] {ECO:0000313|EMBL:KIL52949.1, ECO:0000313|Proteomes:UP000031972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL52949.1,
RC ECO:0000313|Proteomes:UP000031972};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Jeotgalibacillus campisalis genome sequencing.";
RL Submitted (JAN-2015) 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:KIL52949.1}.
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DR EMBL; JXRR01000001; KIL52949.1; -; Genomic_DNA.
DR RefSeq; WP_041053841.1; NZ_JXRR01000001.1.
DR AlphaFoldDB; A0A0C2SG87; -.
DR PATRIC; fig|220754.4.peg.283; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000031972; 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:UP000031972}.
FT DOMAIN 5..391
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 263
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 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 485 AA; 56067 MW; 75F70E84B177330F CRC64;
MERNHTMLQF FEWHVESDGD HWKRLRDAAA DLKANGIDGV WIPPVTKGQS VDDPGYSVYD
LYDLGEFDQK DTVRTKYGTK DELHEAIAAC HENGICVYVD IVMNHKAGAD ETETFQVIEV
DAENRLKEIS EPFDIEGWTK FTFPGREDKY SDFKWNFDHF NGTDWDEKEG RTGFFRILGE
NKSWNDNVDE EFGNYDYLMF ANIDYQHPDV REEMISWGKW LPDTLSCDGF RLDAIKHISH
EFIDEFIREV KDHVDGNFYM VGEYWNNDVE ACGNFLEETN YQLDLFDVML HYNLHEASLK
GNDFDLTTIF HGTLVEKYPL NAVTFVDNHD SQPGESLESW IDDWFKPSAY ALVLLRKDGY
PCMFYGDYFG IGGENSLEGK KEALDPLVYV RAHKAYGQQD DYFDHPNTIG WVRRGEKEFP
HSGCAVVITN GEAGNKKMFV GEQRAGEEWV DYTRSHVDRV KIDEEGFGDF PVQAGSVAVW
SFPGF
//
