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Database: UniProt/TrEMBL
Entry: F5WW47_STRG1
LinkDB: F5WW47_STRG1
Original site: F5WW47_STRG1 
ID   F5WW47_STRG1            Unreviewed;       743 AA.
AC   F5WW47;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   20-JUN-2018, entry version 41.
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:BAK28504.1};
GN   OrderedLocusNames=SGGB_1646 {ECO:0000313|EMBL:BAK28504.1};
OS   Streptococcus gallolyticus (strain ATCC 43143 / F-1867).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981539 {ECO:0000313|EMBL:BAK28504.1, ECO:0000313|Proteomes:UP000007945};
RN   [1] {ECO:0000313|EMBL:BAK28504.1, ECO:0000313|Proteomes:UP000007945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43143 / F-1867 {ECO:0000313|Proteomes:UP000007945};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic
RT   Streptococcus gallolyticus subspecies: genome plasticity, adaptation
RT   and virulence.";
RL   PLoS ONE 6:E20519-E20519(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; AP012053; BAK28504.1; -; Genomic_DNA.
DR   RefSeq; WP_014620207.1; NC_017576.1.
DR   EnsemblBacteria; BAK28504; BAK28504; SGGB_1646.
DR   GeneID; 12630853; -.
DR   KEGG; sgt:SGGB_1646; -.
DR   PATRIC; fig|981539.3.peg.1652; -.
DR   KO; K01176; -.
DR   OMA; FHNAMVG; -.
DR   OrthoDB; POG091H0CDS; -.
DR   BioCyc; SGAL981539:SGGB_RS08435-MONOMER; -.
DR   Proteomes; UP000007945; 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; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 2.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007945};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     39       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        40    743       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003328211.
FT   DOMAIN       49    381       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      391    466       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   743 AA;  81489 MW;  716F10C97A113BBE CRC64;
     MVFRNKEKMK KKLKLGLGSA LIFTILGTGT FVQVSVVNAD TEQVSMKEGT VLHAWCWSFN
     TIKDNMQAIK DAGYTSVQTS PINAVVAGNG GNKSLTNWYY QYQPTVYTIG NYQLGTEEEF
     KEMNRVADQY GIKIIVDAVL NHTTSDYNQI DQQIKSIPNW THGNTQISNW GDRYDVTQSS
     LLGLYDWNTQ NEYVQQYLLN FLKQAVADGA DGFRYDAAKH IELPGEYGSN FWNVILNNGS
     EFQYGEILQD SISNEAGYGQ LMSITASNYG QQIRYALKDR RVAAGNLANY QVSGVDPANL
     VLWVESHDTY ANDDQESTWM SDEDIRLGWA MITARAKGTP LFFSRPVGGG NGTRFTGQSQ
     IGDAGSDLYK DATVAAVNKF HNAMVGESEY IRNPNGDEQV AMIERGSKGA VIVNLVGGDK
     YLDSETNLAD GTYTDQVSGR QFNVSNGRIT GSVPSRSAVV LYDAKDDETV SASIDGYNEG
     NNSISAATEV TLKAKNAQTA TYKIDNGQEV AFQDGDKITV GEGLEAGQST TVTVSATGAD
     GQTASKSYTF TMKDPNAETN IYFQNPDNWS DVYVYMYNAT NTQLLGAWPG TKMTKDSSGR
     YTISVPASYE TEGVKVLFTN NSGAQYPQNT GFDFKAEGVY SKDGLVADVP EGMTRISFDN
     PGGWDSANLY AYYGNPVQMP LGAWPGQAMT KDAQGNFYID LPEEYLDLNV KIIFSQPDTS
     NQFPASIGFD LVKSGNYNKD GLK
//
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