GenomeNet

Database: UniProt
Entry: B7GLU6_ANOFW
LinkDB: B7GLU6_ANOFW
Original site: B7GLU6_ANOFW 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system