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Database: UniProt/TrEMBL
Entry: K4RAV6_9ACTN
LinkDB: K4RAV6_9ACTN
Original site: K4RAV6_9ACTN 
ID   K4RAV6_9ACTN            Unreviewed;       688 AA.
AC   K4RAV6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   20-DEC-2017, entry version 36.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=BN159_6199 {ECO:0000313|EMBL:CCK30578.1};
OS   Streptomyces davawensis JCM 4913.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK30578.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK30578.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4913 {ECO:0000313|EMBL:CCK30578.1,
RC   ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R.,
RA   Blom J., Pelzer S., Kalinowski J., Mack M.;
RT   "Genome Sequence of the Bacterium Streptomyces davawensis JCM 4913 and
RT   Heterologous Production of the Unique Antibiotic Roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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; HE971709; CCK30578.1; -; Genomic_DNA.
DR   RefSeq; WP_015660914.1; NC_020504.1.
DR   EnsemblBacteria; CCK30578; CCK30578; BN159_6199.
DR   GeneID; 31228171; -.
DR   KEGG; sdv:BN159_6199; -.
DR   PATRIC; fig|1214101.3.peg.6281; -.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0CDS; -.
DR   Proteomes; UP000008043; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 2.
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; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF00686; CBM_20; 2.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 2.
DR   SUPFAM; SSF49452; SSF49452; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 2.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008043};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     37       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        38    688       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003879990.
FT   DOMAIN      486    588       CBM20. {ECO:0000259|PROSITE:PS51166}.
FT   DOMAIN      588    688       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   688 AA;  72875 MW;  58DCDAF6E287B5EA CRC64;
     MSRHRPPGAL RRTASLTAAG ALALAGAIAL PAPAAQADAT TSGDVIANLW SYNWDSVAAE
     CTDVLGPNGY GAVWVAPPAE SLKQTNYYWW DVYQPYSYEL SGRFGTAADF ASMVDACHDA
     GVKVYTDAVI NHTAAQTGTG YNGTTISNKY DTPDWDPDDF HTSAECNDSD LIIDDWSNLT
     EIQNCELLGL PDLETEDDDV RSGIAAYLNK QIALGVDGFR IDAAKHMPVA DLNAIWAKLD
     NTTAGAEPYI FQEVYPGSTP AASDYYSAGD VLDFSYASRV KSSFQGNISD LESLPSSGAL
     TPADSVSFVT NHDTERNGLH LSYKDGDTYR LANIFQLAYK WSTPTVYSGF EFSSSDQAPP
     NSNGFVTDTN CASGWYCLQR DTAINGMVKW HNAVGSESVT NWSSKSPSVI GFGRGTAGYV
     AINNGSSAAT YTFATGMADG SYANVVDNGA STVTVSGGNA TLTIPAKSAV AFYDGEFTPC
     DTACEEPDDG TSTVTATFNE YAATSSGQDV YVVGSIAALG NWDTSQAVKL SSSGYPVWSG
     AVSVPVNTSF EFKYIKKDSS GNVTWESNAN RSGATTTSAP AFNNSWNVAS ADATDVTFNV
     TATTDFGTNV YVVGSTASLG SWDTDDAIPL SSASYPTWSK LVIVPKSTAF AYKFIKKDGS
     GNVTWESGTN RSYTTGSSSG YSTADTWK
//
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