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Database: UniProt/TrEMBL
Entry: C5WEL9_STRDG
LinkDB: C5WEL9_STRDG
Original site: C5WEL9_STRDG 
ID   C5WEL9_STRDG            Unreviewed;       467 AA.
AC   C5WEL9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   20-JUN-2018, entry version 63.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amyE {ECO:0000313|EMBL:BAH80834.1};
GN   OrderedLocusNames=SDEG_0325 {ECO:0000313|EMBL:BAH80834.1};
OS   Streptococcus dysgalactiae subsp. equisimilis (strain GGS_124).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=486410 {ECO:0000313|EMBL:BAH80834.1, ECO:0000313|Proteomes:UP000002732};
RN   [1] {ECO:0000313|EMBL:BAH80834.1, ECO:0000313|Proteomes:UP000002732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GGS_124 {ECO:0000313|EMBL:BAH80834.1,
RC   ECO:0000313|Proteomes:UP000002732};
RX   PubMed=21223537; DOI=10.1186/1471-2164-12-17;
RA   Shimomura Y., Okumura K., Murayama S.Y., Yagi J., Ubukata K.,
RA   Kirikae T., Miyoshi-Akiyama T.;
RT   "Complete genome sequencing and analysis of a Lancefield group G
RT   Streptococcus dysgalactiae subsp. equisimilis strain causing
RT   streptococcal toxic shock syndrome (STSS).";
RL   BMC Genomics 12:17-17(2011).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000256|RuleBase:RU361134}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|RuleBase:RU361134}.
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DR   EMBL; AP010935; BAH80834.1; -; Genomic_DNA.
DR   RefSeq; WP_012766561.1; NC_012891.1.
DR   ProteinModelPortal; C5WEL9; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAH80834; BAH80834; SDEG_0325.
DR   KEGG; sds:SDEG_0325; -.
DR   HOGENOM; HOG000008732; -.
DR   KO; K01176; -.
DR   OMA; PYCFGQA; -.
DR   Proteomes; UP000002732; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002732};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:BAH80834.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:BAH80834.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     38       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        39    467       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002958329.
FT   DOMAIN       48    382       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      392    467       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   467 AA;  51394 MW;  FBB13FBA41776C61 CRC64;
     MVAQKTKGLF TKLSIAGLIF GLSNTSLVPL ISTQVVSAES NQIAMKDGAI LHAWCWSFNT
     IKQNMKAIKD ADYTSIQTSP INAVIPGDNG SKDLKNWYFH YQPTDYTIGN YQLGTEDEFK
     AMAAEADKYG INIIVDAVLN HTTTDINAVS EKIKAIPDWT HGNQGITNDY DRYQVTQHAL
     LGLYDLNTQN KAVQEYLLNY LKQAVADGAD GFRFDAAKYI ELPGEFNSDF WTNILANSGA
     KFQYGEVLQG AASRESDYGK LMGVTASHYG EFIRKVIGQG YVKDGDLVNY QVPGVSEDNL
     ITWVESHDNY ANDSEESTKL TDQDIILGWS IIGARKEGVP LFFSRPVGGG GQHGRFPGTT
     KIGDAGSDLF KDPTIVAINK FRNAMNGQSE YTRNPNMDQG LVMIERGGKG AVITNLTSEE
     KRIHSETTLA DGQYKDTITG HIFEVSNKQI SGKMAPRTVA VLYPITQ
//
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