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.
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; 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
//