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Database: UniProt/TrEMBL
Entry: B5FDL2_VIBFM
LinkDB: B5FDL2_VIBFM
Original site: B5FDL2_VIBFM 
ID   B5FDL2_VIBFM            Unreviewed;       460 AA.
AC   B5FDL2;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   20-JUN-2018, entry version 64.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=VFMJ11_1206 {ECO:0000313|EMBL:ACH65452.1};
OS   Vibrio fischeri (strain MJ11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH65452.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J.,
RA   Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R.,
RA   Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001139; ACH65452.1; -; Genomic_DNA.
DR   RefSeq; WP_012533062.1; NC_011184.1.
DR   ProteinModelPortal; B5FDL2; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACH65452; ACH65452; VFMJ11_1206.
DR   KEGG; vfm:VFMJ11_1206; -.
DR   HOGENOM; HOG000274290; -.
DR   KO; K01176; -.
DR   OMA; PYCFGQA; -.
DR   OrthoDB; POG091H0F1O; -.
DR   BioCyc; VFIS388396:G13HN-1207-MONOMER; -.
DR   Proteomes; UP000001857; Chromosome I.
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:UP000001857};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ACH65452.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ACH65452.1}.
FT   DOMAIN       17    378       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   460 AA;  52971 MW;  A546D7D751F9515F CRC64;
     MSQATQQHSD QVPIVSNVIL HAFDWSYQRI TEQAELIAQL GYRSVLVSPA MKSLNLPSGT
     KWWQRYQPQD YRLIDNPLGD TFDFKRMVER LTELNIWVYV DVVFNHMANE SDIRADLEYP
     NQWDREDYAK DPEKYEALTL FGDLSEPLFT ESDFVEAFGI ENWNDKWEVQ NGRISGGPHD
     PGLPTLADNE HVIAQQRAYL KALKAIGVKG FRIDAAKHMS LEHLEKVWDE EITHDIHIFG
     EIITDGGATK EEYETFLSPY LQETKLGAYD FPLFNTLYQA LEGEGSLTSL IDPYIYGMAL
     SPLRAITFAT THDIPNNQVF QDLVMSEENE WLAYAYLFGR DGGIPLIYSE NEISGFKNTE
     GNPRWKDEWC SKRMTQLIGF YHEMYGETQT QVEASDEHLV FARGERGLVA INKSDHNIEV
     NVAVKADIVW LEHTSQTYYA PQQGNLRFFI PAKSYLLFSR
//
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