ID A0A2T1E698_9CYAN Unreviewed; 493 AA.
AC A0A2T1E698;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:PSB28272.1};
GN ORFNames=C7B82_13805 {ECO:0000313|EMBL:PSB28272.1};
OS Stenomitos frigidus ULC18.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Stenomitos.
OX NCBI_TaxID=2107698 {ECO:0000313|EMBL:PSB28272.1, ECO:0000313|Proteomes:UP000239576};
RN [1] {ECO:0000313|Proteomes:UP000239576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC18 {ECO:0000313|Proteomes:UP000239576};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB28272.1, ECO:0000313|Proteomes:UP000239576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC18 {ECO:0000313|EMBL:PSB28272.1,
RC ECO:0000313|Proteomes:UP000239576};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-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:PSB28272.1}.
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DR EMBL; PVWK01000081; PSB28272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1E698; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000239576; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000239576};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 6..402
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 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 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 493 AA; 56332 MW; B0E021F02A50F967 CRC64;
MSELNGVMMQ YFHWYIEPDG KLWKQLAESA DELAKVGVTS VWLPPAYKGT GGGYDVGYGV
YDLFDLGEFD QKGSVRTKYG TKEEYLQAIK VAQKAGIRIY ADAVFNHKLG ADEEEEAQAT
PFSMENRNQP IGEYQTIKAW THFKFPGRKG KYSKMEWHWW HFDAIDYNAY NESERAIYLL
KGKEFDRNVD LENGNFDYLM GCDLDMAHPE VQGELKYWGE WYVDTTGVDG FRFDAVKHVS
ADFFREWLDH VSHYAQRDLF AVGEYWSYDV EALHSFVETT NGRVTLFDAP LHYNFHVASK
AGNSYDMRQI FDNTLVQQQP TLAVTLVENH DSQPLQSLES VVEAWFKPLA YALILLRSEG
YPCIFYADYY GAHYTDKGKD GEDHEVWLDS HRAVLDAMLE ARQTYAYGEQ YDYFDHANTI
GWTRLGDEEH PGGLAVVLSN GSEGTKRMEV KQPNATYVDI TGHVDGAVTT GDDGWGEFRC
NGGSVSVWVP QTK
//
