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Database: UniProt/TrEMBL
Entry: G0CDD4_XANCA
LinkDB: G0CDD4_XANCA
Original site: G0CDD4_XANCA 
ID   G0CDD4_XANCA            Unreviewed;       475 AA.
AC   G0CDD4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=XCR_0920 {ECO:0000313|EMBL:AEL05837.1};
OS   Xanthomonas campestris pv. raphani 756C.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL05837.1, ECO:0000313|Proteomes:UP000001633};
RN   [1] {ECO:0000313|EMBL:AEL05837.1, ECO:0000313|Proteomes:UP000001633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=756C {ECO:0000313|EMBL:AEL05837.1};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V.,
RA   Patil P.B., Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W.,
RA   Aparna G., Rajaram M., Delcher A.L., Phillippy A.M., Puiu D.,
RA   Schatz M.C., Shumway M., Sommer D.D., Trapnell C., Benahmed F.,
RA   Dimitrov G., Madupu R., Radune D., Sullivan S., Jha G., Ishihara H.,
RA   Lee S.W., Pandey A., Sharma V., Sriariyanun M., Szurek B.,
RA   Vera-Cruz C.M., Dorman K.S., Ronald P.C., Verdier V., Dow J.M.,
RA   Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D., Leach J.E.,
RA   White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(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:RU003615}.
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DR   EMBL; CP002789; AEL05837.1; -; Genomic_DNA.
DR   RefSeq; WP_014506694.1; NC_017271.1.
DR   EnsemblBacteria; AEL05837; AEL05837; XCR_0920.
DR   KEGG; xcp:XCR_0920; -.
DR   PATRIC; fig|990315.4.peg.871; -.
DR   KO; K01176; -.
DR   BioCyc; XCAM990315:GLMR-916-MONOMER; -.
DR   Proteomes; UP000001633; 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   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001633};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     35       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        36    475       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003397710.
FT   DOMAIN       36    384       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   475 AA;  51808 MW;  C82DEC7908721D30 CRC64;
     MHATSRPCPR TFWQRAHQLL LIALTLLLTT ASAQADVILH AFNWPYATVE ARAKQIADAG
     YRKVLVAPAY RSEGSAWWAR YQPQDIRLID NPLGDTTAFA RMVQALANNG VETYADVVFN
     HMANEAATRS DLNYPGSAVL AQYAANPGRY DALRLFGTVQ SNFLSGSDFG PAQCISNYND
     AFQVRNYRIC GGGSDPGLPD LLGNDWVVQQ QRAYLQALKG LGVTGFRVDA AKHMTFDHLN
     RVFDAGIRSG VYVFGEVITG GGSGNGDYDQ FLAPYLQSTP HAAYDFPLFN AVRNAFGVGA
     SMQQLVDPAS AGQALPGNRA VTFAVTHDIP NNAGFRYAIL DPVDETLAYA YLLGRNGGVP
     MVYTDNNESG DNRWVNAYLR DDLRRMIGFH NGVQGSDMQV LSSSACHILF RRGSLGIVGI
     NKCGNPVNTT VAMNGSVLFW NADYVDALGS GNVVRISSGS YTFTLPARQA RMWRR
//
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