ID A0A096AZB5_9BACT Unreviewed; 595 AA.
AC A0A096AZB5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=HMPREF2137_03365 {ECO:0000313|EMBL:KGF35912.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF35912.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF35912.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF35912.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361134};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF35912.1}.
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DR EMBL; JRNN01000034; KGF35912.1; -; Genomic_DNA.
DR RefSeq; WP_036872081.1; NZ_JRNN01000034.1.
DR AlphaFoldDB; A0A096AZB5; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000029556; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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; PF00128; Alpha-amylase; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..595
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001916790"
FT DOMAIN 29..350
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 595 AA; 67235 MW; F57385B46F571B02 CRC64;
MKLFKTFLFL FLAIPAPFFA QGWPKDYKGV MLQAFYWDSY SDTQWTNLES QADELSQYFD
LIWVPQSGYC NKLQDQMGYA PIWWFNHKSA FGTEDQLRKM IKTFKEKGTG IIEDVVINHR
NGNTNWCNFP EETWKGQTMH WSLADICQND DGGNTKRNGY DVSGAMDTGD DFSGCRDLDH
TSDNVRKNVK LYLRFLKEEL GYTGFRYDMV KGFSAKYIGE YNASAQPTYS VGEYWDGDPA
KLKSWLDGTK VDGKIQSAAF DFALKYYIKD ALGSGQWNRL DGDCPAKDPA YSRYAVTFVD
NHDTDRDNNR LVANYIAANA YIMAMPGTPC VFLTHWKQYK TQLKKLILAR KAAGISNQSA
ILKSERHGNG YIVNVRGEKG NVLLALGTPD SYDANGYKIA VEGDGYKYYV ADNVDISAVQ
AIADEEPQAF TPPAFCTIDN DERCAFFEAP SFWTGTVNCW QWDQKANYTG GSWPGVACRY
VGTTKAGNKV YKWSWNKQTK PANNPDAGII FNCDNGSKQT ANLEFVNGGY YDFTSGKKGV
VTGINKVIST QTDQRKVNVY ALDGRLVRSQ VSENKSLQGL QRGVYVVNRR KLFVR
//
