ID A0A0Q8AQV9_9MICO Unreviewed; 553 AA.
AC A0A0Q8AQV9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=ASD56_01185 {ECO:0000313|EMBL:KQZ85017.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ85017.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ85017.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ85017.1,
RC ECO:0000313|Proteomes:UP000051650};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ85017.1}.
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DR EMBL; LMGL01000001; KQZ85017.1; -; Genomic_DNA.
DR RefSeq; WP_055960301.1; NZ_LMGL01000001.1.
DR AlphaFoldDB; A0A0Q8AQV9; -.
DR STRING; 1736478.ASD56_01185; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000051650; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051650}.
FT DOMAIN 22..420
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 400..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 62708 MW; 0A6107729F6EE01F CRC64;
MKITDTSDLW WKTSVVYCLD VETYLDHDGD GVGDFAGLAQ RIDYLADLGV TCLWLMPFYP
TADRDDGYDV TDFYGVDPRL GTHGDVVEVI RTARDRGIRV IVDLVVNHTA DTHPWFVAAR
RSRNSRYRDY YVWRDEPPAN NVNTVFPGEE TTLWELDEKS GQYYLHTFYR HQPDLNIGNP
AVRDEIAKTI GFWLQLGISG FRVDAVPFLI EVPEGEDLAD PHEYLRDLRR FLRRRSREAV
LLGEVNLPYK EQLDYFGDNQ GEELTLQFDF IGMQALYLSL ARSDPRPLAK ALRARPAIAP
EAQWANFVRN HDELTLDKLT DAEREEVFAA FAPDERQRVY GRGITRRLPT MLGGDPRRIR
MVYSLLFSLP GVPVLFYGEE IGMGENPDIL GRTSVRTPMQ WSDSRNGGFS PAAPSRLTSR
PPEGGYAPEH INASQQLNDD ESLLHFIRKL AARYRISPEI GWGTAELLEH DAPSVLVHSV
RADVGRMVAL HNFADEPARV RLALEDEPEG AELTDLFGPD RLALGPAGRV ELDLPAYGWR
WLRVARPGDG RLG
//
