GenomeNet

Database: UniProt/TrEMBL
Entry: D7CD09_STRBB
LinkDB: D7CD09_STRBB
Original site: D7CD09_STRBB 
ID   D7CD09_STRBB            Unreviewed;       460 AA.
AC   D7CD09;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amyA2 {ECO:0000313|EMBL:ADI10856.1};
GN   OrderedLocusNames=SBI_07736 {ECO:0000313|EMBL:ADI10856.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI10856.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI10856.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI10856.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002047; ADI10856.1; -; Genomic_DNA.
DR   RefSeq; WP_014180306.1; NC_016582.1.
DR   AlphaFoldDB; D7CD09; -.
DR   STRING; 749414.SBI_07736; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; sbh:SBI_07736; -.
DR   PATRIC; fig|749414.3.peg.7956; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_0_0_11; -.
DR   OMA; FRYAYDL; -.
DR   Proteomes; UP000000377; 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: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:UP000000377};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..460
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003094239"
FT   DOMAIN          35..372
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          381..457
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   460 AA;  49601 MW;  CD74D5E7F6371BF3 CRC64;
     MASRPLAAAL ALAAGAAMLI ALPGQAQAAP PGDKDVTAEL FEWTYASVAK ECTSTLGPAG
     YGYVEVSPAT EHIQGGQWWT SYQPVSYKIA GRLGDRTAFK NMIDTCHAAG VKVVADAVIN
     HMSAGSGTGT GGSSYTKYTY PGIYQSQDMD DCTAQISNYQ DRWNVQRCEL VGLADLDTGE
     SYVRDRIAQY LNDLLSLGVD GFRIDAAKHM AAEDLAAIKS KLSNPNVYWK QEAIYGAGEA
     VSPTEYLGNG DVQEFRYGRD LKRVFTSEKL AYLNNFGEGW GYMASGKSGV FVDNWDTERN
     GSTLSYKDNA NYTLANVFML AWPYGSPDVH SGYEFSDNDA GPPNGGTVNA CWQDGWKCQH
     KWPEIIKMVA FRNTARGATV TNWWDNGNNA IAFGRGEKAY VAINHEDTSL TRTFQTSLPA
     GGYCDVQSGR SVTVDSSGQF TATLGANTAV ALHVGARSCG
//
DBGET integrated database retrieval system