ID A0A1I0VRJ0_9BACL Unreviewed; 571 AA.
AC A0A1I0VRJ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=SAMN05216312_101469 {ECO:0000313|EMBL:SFA78510.1};
OS Cohnella sp. OV330.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFA78510.1, ECO:0000313|Proteomes:UP000198686};
RN [1] {ECO:0000313|EMBL:SFA78510.1, ECO:0000313|Proteomes:UP000198686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV330 {ECO:0000313|EMBL:SFA78510.1,
RC ECO:0000313|Proteomes:UP000198686};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKE01000001; SFA78510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VRJ0; -.
DR Proteomes; UP000198686; 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; cd11316; AmyAc_bac2_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:SFA78510.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000198686}.
FT DOMAIN 56..439
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 395..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 61436 MW; 707BC5EA549800BA CRC64;
MQGETGADAG ERGAAVRKLR RIVTAAAAVG ALGSLLVSCS TVKTEDAKGP SGVYYEIFVR
SFADSNGDGI GDIKGIEQKL DYLEELGVDG LWLTPIQPSP SYHGYDVTDY YGINPQFGTM
DDYKSLLAAA HKHGMKVLMD LVVNHTSAEH PWFAASASGK DDAHRNWYTW AEDRGLSTSA
MSATGGEAWH AVGGGDHYLG TFWSGMPDLN FDEPAVRAEM IKIGNYWLDQ GVDGFRLDAA
KHVYEDFKSQ ANSPAVAKKN QAWWQEFRRG LTAKHPDVYL VGEVWSSAGA IVPYVKNALD
STFDFDLSDW IRDAAAKGTA SDMPSRLERT SEIFARESGG KYIDAPFLDN HDRDRFMSLA
GGDVAKGKLA AAMLLTMPGR PFVYYGEEFG MQGAGADERK REPMRWTKSG ADPDSSQAGE
GRTNAGEGQS NAGKGGAIRE PSEAGTGQTR WEPSVANTDP AVSVEAQDGE AGSMLSRYRE
LIALRGQSAA LRDGAIVPVA AEPPAGTVAF IRATAEERVY VAHNLTAEPK TIALDAESAK
AYRKLWYASE SGAGLKEGTI TLPAYGTVIL K
//
