ID A0A1G8YMX5_9ACTN Unreviewed; 567 AA.
AC A0A1G8YMX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=SAMN05421806_104157 {ECO:0000313|EMBL:SDK04086.1};
OS Streptomyces indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=417292 {ECO:0000313|EMBL:SDK04086.1, ECO:0000313|Proteomes:UP000199155};
RN [1] {ECO:0000313|EMBL:SDK04086.1, ECO:0000313|Proteomes:UP000199155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDK04086.1,
RC ECO:0000313|Proteomes:UP000199155};
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|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; FNFF01000004; SDK04086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8YMX5; -.
DR STRING; 417292.SAMN05421806_104157; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000199155; 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; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd05808; CBM20_alpha_amylase; 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; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
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; 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 Pfam; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 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:UP000199155};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..567
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011484088"
FT DOMAIN 466..567
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 567 AA; 60041 MW; 00BC01ACE73D5CE2 CRC64;
MARGRQLLGA IGAIGLGLGL TVAAPTPAQA APLGGKDVTA VLFEWRFASV AKACTEDLGP
AGYGYVQVSP PQEHIQGSQW WTSYQPVSYK IAGRLGDRTA FKNMVDTCHA AGVKVVADSV
INHMAAGDGT GTGGSGYTKY NYPGIYSGAD MDDCRAQIGN YGDRGNVQNC ELVGLADLDT
GEPYVRERIA AYLNDLLSLG VDGFRIDAAK HMPAGDLANI KSRLSDPNVY WKQEAIYGGG
EAVSPSEYLG NGDVQEFRYA RGLKQTFLNE NLANLKNYGE GWGFMESGKS AVFVDNHDTE
RGGDTLSYKN GSAYTLANVF MLAWPYGSPD VHSGYEWSDK DAGPPNSGTV NACYADGWKC
QHDWREISSM VAFRNEARGQ SVTNWWDNGG DQIAFGRGSK AYVAINHEGS ALTRTFQTSL
PAGDYCDVQS GMGVSVNGSG QFTATVPAGT AVALHTGARS CTGTPGPDPV STGASFNVHA
TTVMGQNIHV VGDCAQLGGW NTGSAPKLDP ASYPVWKLDV ALPAGTTCAY KYLRKDASGA
VTWESGVNRT LTVPASGAVT LNDTWRA
//
