ID A0A098ME93_9BACL Unreviewed; 845 AA.
AC A0A098ME93;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=PWYN_01430 {ECO:0000313|EMBL:KGE20869.1};
OS Paenibacillus wynnii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=268407 {ECO:0000313|EMBL:KGE20869.1, ECO:0000313|Proteomes:UP000029734};
RN [1] {ECO:0000313|EMBL:KGE20869.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE20869.1,
RC ECO:0000313|Proteomes:UP000029734};
RA den Bakker H.C.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE20869.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE20869.1,
RC ECO:0000313|Proteomes:UP000029734};
RA Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (OCT-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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KGE20869.1}.
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DR EMBL; JQCR01000001; KGE20869.1; -; Genomic_DNA.
DR RefSeq; WP_036647608.1; NZ_JQCR01000001.1.
DR AlphaFoldDB; A0A098ME93; -.
DR STRING; 268407.PWYN_01430; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG2819; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000029734; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 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; 3.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03423; CBM_25; 1.
DR Pfam; PF00041; fn3; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM01066; CBM_25; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000029734};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..845
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001938160"
FT DOMAIN 562..647
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 738..844
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 845 AA; 91015 MW; E5CE931C099E2EFA CRC64;
MKRKLWLLPV LITSMVLSLA IQLFVLTPSV AEAASIGTVT ENDSIYQIMV DRFNDGDSTN
NATGSAIRYG ETTEDDFRYM KGGDWQGVID KLPYIKNMGY TAIWISPVAE PQMTNRDNNG
TGKNTAYHGY NVKNPNAANP YFGTKEKLKE LVDAAHAQGI KVIIDVVPNH IGDYMLGTQA
NYDIASLQPV APFNNPSWYH HNGDINWGLV DGRYDQWAQD YLENHDLGGL DDIDFDVPAA
KQAIFNSIKG WFDYTGADGA RVDAAKLIKP TDIGELQNLL GVNTFGENFD GNAEFVSRWV
GTNKEWGMLD FPLFFSVLNS FAYGQSFDAN IKSTLAQDSV YNGNANHMVT FIDNHDRNRF
LTEAGGNVAK MQNALAFLFT VRGTPVVFQG TEQDKGNGNG QIMTGGIADT WNRWSMVKRD
ANGNVLQNYF NENANTYKFV AKLNDIRKNN AALRTGTQRE MWSAQNLYAF SRRVDSGANL
GQEVISVFSN ASSGTQSVNL PLRAESTLTV GTVLVNQLNT ADTVTVQSGG ATGKQIAVSV
GANASKIYAK QPLIVDTIAP TPPTNVTAVP QSASSVLVSW TASTDNVGVT GYEVYRNGVK
VGTTAATSYT DINLTSSTTY EYTIKAFDAA GNLSGLSAIA FATTPPGNSV KIFYKNPAFS
SSYIHYKLDG ATTWTTPPGV QMSSSAFSGY SVITVPLGSS AGLTAAFNNG SGTWDSNGSS
NYHFNSGTWS LVNGSISAGE PKADGVTFRV TVPSTTPASG PVYLTGSFNN WNAADPAYQL
TKGSDGIYSI TLNLPAGTAV QYKLTRGTWA TVETTTSGAD IANRTLTPSG GAQTVTLTVQ
RWKDQ
//
