ID B7GLU6_ANOFW Unreviewed; 505 AA.
AC B7GLU6;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN OrderedLocusNames=Aflv_2188 {ECO:0000313|EMBL:ACJ34547.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34547.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ34547.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP000922; ACJ34547.1; -; Genomic_DNA.
DR RefSeq; WP_012575725.1; NC_011567.1.
DR AlphaFoldDB; B7GLU6; -.
DR STRING; 491915.Aflv_2188; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 7038441; -.
DR KEGG; afl:Aflv_2188; -.
DR PATRIC; fig|491915.6.peg.2247; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_7_3_9; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11339; AmyAc_bac_CMD_like_2; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000742};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..505
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002856220"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..384
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 505 AA; 59025 MW; FCFD03DAE7745E00 CRC64;
MKRVFRALLI FVLLLSVTAP VSAKTERTWQ DERVYFIMVD RFNNGNPKND YEVNVHDPKA
YHGGDLQGII DKLDYIKGMG FTAIWLTPIF ANEKGGYHGY WIEDFYKVEE HFGTLDDFKR
LVKEAHKRDM KVILDFVVNH TGYNHPWLND PAKKEWFHEK KDIFNWANQQ EVENGWLFGL
PDLAQENPEV KAYLFDVAKW WIQQTDIDGY RLDTVKHVPK WFWDEFAKEV KSVKQDFFLL
GEVWHDDPRY VAEYGKHGID ALIDFPFYKE ASTIFSNVDQ SLEPLYNVWK RNEAFYDRPY
LLGTFLDNHD TVRFTRLALQ NRINPVTRLK LGLTYLFSAP GIPIMYYGTE IALDGGEDPD
NRRLMNFRTD KELVDYVTKL GELREKLPSL RRGDFELLYE KDGMALFKRT YEKETTVIAI
NNTSKTQKVT LDDELEQGKE LRGLLAGDLV RSKDGKYDII LDRETAEIYV LAPKTGLNIP
FIAALVAVYT AFGLFLYFAR KRKAS
//