ID B0B0V6_STRGA Unreviewed; 569 AA.
AC B0B0V6;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 Name=gacE2 {ECO:0000313|EMBL:CAL64868.1};
GN ORFNames=SGLAU_00940 {ECO:0000313|EMBL:AIR96216.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:CAL64868.1};
RN [1] {ECO:0000313|EMBL:CAL64868.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GLA.O {ECO:0000313|EMBL:CAL64868.1};
RX PubMed=19059289; DOI=10.1016/j.jbiotec.2008.10.016;
RA Rockser Y., Wehmeier U.F.;
RT "The gac-gene cluster for the production of acarbose from Streptomyces
RT glaucescens GLA.O: identification, isolation and characterization.";
RL J. Biotechnol. 140:114-123(2009).
RN [2] {ECO:0000313|EMBL:AIR96216.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GLA.O {ECO:0000313|EMBL:AIR96216.1};
RA Ortseifen V., Albersmeier A., Winkler A., Puhler A., Kalinowski J.,
RA Ruckert C.;
RT "Complete genome sequence of the Actinobacterium Streptomyces glaucescens
RT GLA.O (=DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
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; CP009438; AIR96216.1; -; Genomic_DNA.
DR EMBL; AM409314; CAL64868.1; -; Genomic_DNA.
DR RefSeq; WP_043497452.1; NZ_CP009438.1.
DR AlphaFoldDB; B0B0V6; -.
DR STRING; 1907.SGLAU_00940; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; sgu:SGLAU_00940; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_013336_3_1_11; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000029482; Chromosome.
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:UP000029482};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..569
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010821607"
FT DOMAIN 468..569
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 60586 MW; 46F42927B3AC3F04 CRC64;
MANKTVATAL ALVAGAAVVV TAPGTAQADP PGGKDVTAVM FEWNFASVAK ACTDDLGPAG
YGYVQVSPPN ERVPGPQWWT AYQPVSYRIA TKLGGRDAFK SMIDTCHAAG VKVVVDTVIN
HMANSAGTGT GGSSYSKYDY PGLYSKSDMD DCMKDIDNYG NSWNVHHCEL SGLPDLDTGE
EYVRKTIAGY LNDLLSLGVD GFRIDAAKHI PPADLADIKG RLRDPGVYWK QETIGAYGEA
VQPAQYTGTG DVQEFSYGRD LKRVFSGEKL AYLKNLGEAW GYVAGDKAAT FVTNHDTERH
NATLTYKDGA KYTLAHVFML AWPYGSPDVH SGYQFSDDAG SPNNGRVDAC YTDGWKCQHA
WREIAGMVGF RNTAGSAEVT DWWDNGSNAI AFGRGSKAYV AINHESGSLT RTFQTSLPAG
TYCDVQSGKP VTVNGSGQFT ATLGPDTALA LHTGATSCTD PGGGNPGENP GEDPGASFAV
QAPTTWGENI YVTGNRSALG DWNPAGALKL DPAAYPVWKL DVALPAGTSF EYKFLRKDAS
GKVTWESGPN RTATVPSSGR TLLSDTWRG
//
