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Database: UniProt/TrEMBL
Entry: A0KGI8_AERHH
LinkDB: A0KGI8_AERHH
Original site: A0KGI8_AERHH 
ID   A0KGI8_AERHH            Unreviewed;       858 AA.
AC   A0KGI8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   31-JAN-2018, entry version 81.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=AHA_0837 {ECO:0000313|EMBL:ABK39061.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39061.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39061.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39061.1; -; Genomic_DNA.
DR   RefSeq; WP_011704783.1; NC_008570.1.
DR   RefSeq; YP_855379.1; NC_008570.1.
DR   ProteinModelPortal; A0KGI8; -.
DR   STRING; 380703.AHA_0837; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABK39061; ABK39061; AHA_0837.
DR   GeneID; 4487124; -.
DR   KEGG; aha:AHA_0837; -.
DR   PATRIC; fig|380703.7.peg.836; -.
DR   eggNOG; ENOG4105E54; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   HOGENOM; HOG000272352; -.
DR   KO; K01176; -.
DR   OMA; WKCQHAW; -.
DR   Proteomes; UP000000756; 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; -; 4.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00801; PKD; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF49299; SSF49299; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ABK39061.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ABK39061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    858       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002625709.
FT   DOMAIN      577    661       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      577    660       PKD. {ECO:0000259|PROSITE:PS50093}.
SQ   SEQUENCE   858 AA;  91578 MW;  E526803D9E6AF656 CRC64;
     MHSTLLRTAL LTAALGSFSH TATAEGVMVH LFQWKFNDIA NECETVLGPK GFGGVQITPP
     AEHKQGSQVW WTVYQPVSFK NFNSFGGSEA ELRSMIARCN AAGVKVYADA VFNQLASGSG
     TATGGGSYNA GQYQYPQFGY NDFHHSGDIT NYGDSNNVWN GALYGMPDLN TGSPYVQDQI
     ATYMKTLLGW GVAGFRIDAA KHMAPTDVKA ILDKAGSPKA YLEVIGAGGE SPDIQPGRYT
     YIDTVTDFKY GTDLAANFNG QIKNLKTLGE SWGLLPSAKA FVFVVNHDRE RGHGGGGMLT
     FMSGARYDLA NTFMIAWPYG WKQVMSGYRF ENMSTYETDK GAPGSTPCTD SQWNCEQRRP
     TIMNMALFHN RTEGQPVSNW WDNGNNQIAF GRGDKGFVAI NNESGSLVAS LQTALPAGEY
     CNLLGGNDYC SGGYVTVDGS GKASLNVPGM KAAAIIAGCT KASPCGGSAL PGTKFSSMNL
     RGTHNAWGNT PMTVDANRVW SATLTLTGNG DATGAQRFKF DVFGNWAENY GDNEGDGIAD
     KGSSKDILVS GAGSYRITLN ESDLRYTVTP LTSNQAPVAA LSPKTLSVKA GESVVFDASA
     SHDDGGVVSY SWSSGGTAAT ETVRFDTPGT YTVTVTVTDA EGLTASASAT VTVTDDNGTY
     TSVLPTLNFR GTPNAWGSLA MTLVADNQWE ALVTFNGQAN QRFKFDVKGD WSKNYGDTNK
     DGVAELAGSD ILTSVTGQYR VRFNDQTLQY SLTPVSVGYA KNFASLNIRG TTNNWGSTPM
     SLVGDHLWQA SVTFTGSGDG NGGQRFKFDV KGDWTQNYGD TNRDGVAEQA GADITTALVG
     VYVVRFNDQT LAYSLNAQ
//
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