ID A0A3S3ZHB6_9MICO Unreviewed; 550 AA.
AC A0A3S3ZHB6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=ELQ90_16415 {ECO:0000313|EMBL:RWZ46065.1};
OS Labedella phragmitis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=2498849 {ECO:0000313|EMBL:RWZ46065.1, ECO:0000313|Proteomes:UP000288547};
RN [1] {ECO:0000313|EMBL:RWZ46065.1, ECO:0000313|Proteomes:UP000288547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11W25H-1 {ECO:0000313|EMBL:RWZ46065.1,
RC ECO:0000313|Proteomes:UP000288547};
RA Li F.;
RL Submitted (DEC-2018) 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:RWZ46065.1}.
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DR EMBL; RZNB01000010; RWZ46065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3ZHB6; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000288547; 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; cd11334; AmyAc_TreS; 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; 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:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 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};
KW Hydrolase {ECO:0000256|RuleBase:RU361134}.
FT DOMAIN 22..412
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 550 AA; 62956 MW; 36EC99525399A9C5 CRC64;
MKVTDTSDLW WKTAVVYNLD VETYLDWNDD GVGDFEGLAH RIDYLAELGV TCLWLAPFYP
SPQKDNGYDI TDYYGVDPRY GHLGDVVEVF RTAKDRGIRI IVDLVVNHTS DQHPWFREAL
KGKDNPYRDY YRWRDTPPKN QKENAFPDTE DGTWFLDEKS GQYYRHSFYR HQPDLNTANP
VVRDEIAKII GFWFQLGVDG FRVDAVPYLL DDDTPDDPYD FLRTVRRYVG RRSGTGMLLG
EVNLPHHEQF GFFGAEDGDG LTMQFDFVTN QALYLALARE DARPIATSLQ SRPVLASSNQ
WGNFVRNHDE LNLNQLSEEE RQFVFEKFAP EESMRLHGRG IRRRLPPLID SDPRRLAMVY
SLIFSLPGAP VLYYGEEIGM GENLDLSGRE SVRSPMQWSD QENGGFSSAP KRKLVTAVTE
GGFGPEYVNA AQQRHADSSL FTFIRTLVQA YRNSPEIGWG EFALLEQPHD AVLAHSLRTD
TGHLVALHNL GSEAHTVPIT LERIEPESRV VDLFHDHVLQ PDGKGQLEVP LDGYGHRWFR
VVRPGDKRLT
//
