ID K4LYT6_9BACI Unreviewed; 516 AA.
AC K4LYT6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AFV13099.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:AFV13099.1};
OS Bacillus sp. 406.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1235853 {ECO:0000313|EMBL:AFV13099.1};
RN [1] {ECO:0000313|EMBL:AFV13099.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=406 {ECO:0000313|EMBL:AFV13099.1};
RA Kachan A.V., Rus O.B., Evtushenkov A.N.;
RT "A.V. Kachan, O.B. Rus, A.N. Evtushenkov. Cloning of the alpha-amylase gene
RT from Bacillus sp. 406 and analysis of its nucleotide and amino acid
RT sequences.";
RL Tr Beloruss Gos Univ Ser Fiziol Biohim Mol Osn Funkc Sist 4:174-181(2009).
RN [2] {ECO:0000313|EMBL:AFV13099.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=406 {ECO:0000313|EMBL:AFV13099.1};
RA Comotor D., Becsagh P., Rakhely G., Schneider G., Kovacs T.;
RL Submitted (JUL-2012) 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; JX429073; AFV13099.1; -; Genomic_DNA.
DR AlphaFoldDB; K4LYT6; -.
DR SMR; K4LYT6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:AFV13099.1};
KW Hydrolase {ECO:0000313|EMBL:AFV13099.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..516
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039185137"
FT DOMAIN 36..424
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 294
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 516 AA; 58352 MW; 361E410D5D175DDA CRC64;
MRTKSSRTWF SLLLALLIFV PTVAPNHKAE AAAQNGTMMQ YFEWYVPNDG QHWNRLRNDA
AYLKSIGVSA VWTPPAYKGT SQNDVGYGAY DLYDLGEFNQ KGTIRTKYGT KAELKSAVST
LKSNGIQVYG DVVMNHKGGA DYTENVTAVE VNPSNRNQET SDEYTIQAWT GFNFPGRGTT
HSPFKWQWYH FDGTDWDQSR NASRIFKFRG TGKAWDWEVS SENGNYDYLM YADLDFDHPD
VGNEMKNWGV WYANEVGLDG FRLDAVKHIK HSYLGDWVNH VRTKTGKEMF TVAEYWQNDV
NAINNYLAKV NYNHSVFDAP LHYNFHYASQ SGGNYDMRNL LNGTVVAAHP TKAVTLVENH
DSQPGQSLES VVQPWFKPLA YAFILTRAEG YPSIFYGDMY GTKGNSSYEI PALKTKIEPL
LKARKDYAYG TQHNYMDHWD VIGWTREGDS TKEKSGLATL VTDGAGGSKW MYVGKQNAGE
VWYDITGNRT DKITINTDGW GNFQVNGGSV SVYGQQ
//
