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Database: UniProt/TrEMBL
Entry: G2LSY7_9XANT
LinkDB: G2LSY7_9XANT
Original site: G2LSY7_9XANT 
ID   G2LSY7_9XANT            Unreviewed;       452 AA.
AC   G2LSY7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 39.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=XACM_0793 {ECO:0000313|EMBL:AEO41097.1};
OS   Xanthomonas axonopodis pv. citrumelo F1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=981368 {ECO:0000313|EMBL:AEO41097.1, ECO:0000313|Proteomes:UP000001276};
RN   [1] {ECO:0000313|EMBL:AEO41097.1, ECO:0000313|Proteomes:UP000001276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:AEO41097.1};
RX   PubMed=21908674; DOI=10.1128/JB.05777-11;
RA   Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H.,
RA   Setubal J.C., Wang N.;
RT   "Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo
RT   F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains
RT   Provides Insights into Virulence and Host Specificity.";
RL   J. Bacteriol. 193:6342-6357(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; CP002914; AEO41097.1; -; Genomic_DNA.
DR   EnsemblBacteria; AEO41097; AEO41097; XACM_0793.
DR   KEGG; xax:XACM_0793; -.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0F1O; -.
DR   Proteomes; UP000001276; 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:UP000001276};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134}.
FT   DOMAIN       13    361       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   452 AA;  49363 MW;  173B99F0EE053AA6 CRC64;
     MVLLLTTANA QADVILHAFN WPYATVEARA KQIADAGYRK VLVAPAYRSE GSAWWARYQP
     QDIRLIDNPL GDTAAFKKMV QALANNGVET YADIVFNHMA NEAATRSDLN YPGSAVLSQY
     AANPGRYDSL RLFGTLQSNF LSASDFGPAQ CISNYNDAYQ VRNYRICGGG SDPGLPDLVG
     NDWVVQQQRA YLQALKSIGV TGFRVDAAKH MTFDHLNRVF DAGIRSGVYV FGEVITGGGT
     GNGDYDQFLA PYLQSTPHAA YDFPLFNAVR NAFAIGASMQ QLVDPAASGQ ALPGNRAVTF
     AVTHDIPNNA GFRYAILDPV DETLAYAYLI GRNGGMPMIY TDNNESGDNR WVNAYLRDDL
     RRMIGFHNGV QGTDMQVLSS SSCHILFRRG SLGIVGINKC GNPVTTTVGM NNSVLYWNAD
     YVDALGSGNV VRISSSSYTF TLPARGARMW RR
//
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