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Database: UniProt
Entry: Q59222_9BACI
LinkDB: Q59222_9BACI
Original site: Q59222_9BACI 
ID   Q59222_9BACI            Unreviewed;       613 AA.
AC   Q59222;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AAA63900.1};
DE            EC=3.2.2.1 {ECO:0000313|EMBL:AAA63900.1};
GN   Name=Amy {ECO:0000313|EMBL:AAA63900.1};
OS   Bacillus sp. TS-23.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=38441 {ECO:0000313|EMBL:AAA63900.1};
RN   [1] {ECO:0000313|EMBL:AAA63900.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TS-23 {ECO:0000313|EMBL:AAA63900.1};
RA   Lin L.-L., Chu W.S., Hsu W.H.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; U22045; AAA63900.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59222; -.
DR   SMR; Q59222; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008477; F:purine nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
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   Pfam; PF00686; CBM_20; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:AAA63900.1};
KW   Hydrolase {ECO:0000313|EMBL:AAA63900.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          510..612
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   613 AA;  69537 MW;  14684A30FC2895E8 CRC64;
     MNNVKKVWLY YSIIATLVIS FFTPFSTAQA NTAPINETMM QYFEWDLPND GTLWTKVKNE
     AANLSSLGIT ALWLPPAYKG TSQSDVGYGV YDLYDLGEFN QKGTIRTKYG TKTQYIQAIQ
     AAKAAGMQVY ADVVFNHKAG ADGTEFVDAV EVDPSNRNQE TSGTYQIQAW TKFDFPGRGN
     TYSSFKWRWY HFDGTDWDES RKLNRIYKFR STGKAWDWEV DTENGNYDYL MFADLDMDHP
     EVVTELKNWG TWYVNTTNID GFRLDAVKHI KYSFFPDWLT YVRNQTGKNL FAVGEFWSYD
     VNKLHNYITK TNGSMSLFDA PLHNNFYTAS KSSGYFDMRY LLNNTLMKDQ PSLAVTLVDN
     HDTQPGQSLQ SWVEPWFKPL AYAFILTRQE GYPCVFYGDY YGIPKYNIPG LKSKIDPLLI
     ARRDYAYGTQ RDYIDHQDII GWTREGIDTK PNSGLAALIT DGPGGSKWMY VGKKHAGKVF
     YDLTGNRSDT VTINADGWGE FKVNGGSVSI WVAKTSNVTF TVNNATTTSG QNVYVVANIP
     ELGNWNTANA IKMNPSSYPT WKATIALPQG KAIEFKFIKK DQAGNVIWES TSNRTYTVPF
     SSTGSYTASW NVP
//
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