ID   A0A1C5H1S8_9ACTN        Unreviewed;       482 AA.
AC   A0A1C5H1S8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=GA0070609_0786 {ECO:0000313|EMBL:SCG39883.1};
OS   Micromonospora echinaurantiaca.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47857 {ECO:0000313|EMBL:SCG39883.1, ECO:0000313|Proteomes:UP000198217};
RN   [1] {ECO:0000313|EMBL:SCG39883.1, ECO:0000313|Proteomes:UP000198217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43904 {ECO:0000313|EMBL:SCG39883.1,
RC   ECO:0000313|Proteomes:UP000198217};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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|ARBA:ARBA00000548,
CC         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}.
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DR   EMBL; LT607750; SCG39883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5H1S8; -.
DR   Proteomes; UP000198217; Chromosome i.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198217};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..482
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039267210"
FT   DOMAIN          39..385
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          394..480
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   482 AA;  52695 MW;  9F5C468F4A2343E1 CRC64;
     MHRRRWHSAL LALGVIASVL VPTTVTAPPA VAAPAGAKKV IVQLFEWNWT SVANECRTTL
     GPKGYGWVQV SPPQEHVRGS QWWLAYQPVN YRIESRKGTR AQFKAMVDAC HAAGVKVIVD
     AVVNHMSGQD NGGTGWAGSS YGHYDYPGIY QYQDFHHCGR NGGDDIANYG DRWEVQNCEL
     VNLADLKTES DYVRGRLAGY LNDLLSLGVD GFRMDASKHM PAADIAALRS RLSRPAYLVQ
     EVIHGAGEPI QPGEYTGNGD VHEFRYGKDL ARVFRSERLA YLRNFGEGWG HLPGGVAAVF
     VDNHDTQRDV GGVLTYRDRG SYALANAFML AWPYGSPTVM SSYTFSQRDQ GPPQDGSGRT
     LDVTCYSGWE CEHRWPVIAN MVGFRNATEG AAVANWYDNG NNHIAFSRTG KGYLTVNDED
     HAITGRSYHA GLPAGRYCDV IHGTFSNGSC SGPVITVDGN GWFAANIPAH DAVAIHVGAR
     LS
//