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Database: UniProt/TrEMBL
Entry: F4F410_VERMA
LinkDB: F4F410_VERMA
Original site: F4F410_VERMA 
ID   F4F410_VERMA            Unreviewed;       482 AA.
AC   F4F410;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   18-JUL-2018, entry version 42.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=VAB18032_27916 {ECO:0000313|EMBL:AEB46656.1};
OS   Verrucosispora maris (strain AB-18-032).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Verrucosispora.
OX   NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB46656.1, ECO:0000313|Proteomes:UP000008308};
RN   [1] {ECO:0000313|EMBL:AEB46656.1, ECO:0000313|Proteomes:UP000008308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB46656.1,
RC   ECO:0000313|Proteomes:UP000008308};
RX   PubMed=21551311; DOI=10.1128/JB.05041-11;
RA   Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M.,
RA   Bull A.T., Kim K.H., Bibb M.J., Choi I.G., Stach J.E.;
RT   "Genome sequence of the abyssomicin- and proximicin-producing marine
RT   actinomycete Verrucosispora maris AB-18-032.";
RL   J. Bacteriol. 193:3391-3392(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; CP002638; AEB46656.1; -; Genomic_DNA.
DR   RefSeq; WP_013735306.1; NC_015434.1.
DR   STRING; 263358.VAB18032_27916; -.
DR   EnsemblBacteria; AEB46656; AEB46656; VAB18032_27916.
DR   KEGG; vma:VAB18032_27916; -.
DR   eggNOG; ENOG4105E54; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OMA; WKCQHAW; -.
DR   OrthoDB; POG091H0CDS; -.
DR   BioCyc; VMAR263358:GI1P-4665-MONOMER; -.
DR   Proteomes; UP000008308; 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; 2.60.40.1180; -; 1.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008308};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008308};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33    482       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003313576.
FT   DOMAIN       39    385       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      394    480       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   482 AA;  53176 MW;  C4DB505DA1401A6D CRC64;
     MHRRRLRTAI VALGTITTLL APTVVTAPPA VAAPTGGKKV IANLFEWNWP SVASECASTL
     GPKGYGYVQV SPPQEHVRGN QWWVAYQPVS YRIESRKGTR DQFRSMVATC QAAGVKVIVD
     AVINHMSGQT NGGTGWAGSS YQHHVYPGIY QAQDFNYCGR NGNNDIVNYN DRYEVQNCEL
     VNLADLKTGS DYVRSRLAAY LNDLLSLGVD GFRLDASKHM PAADIANILS RLNRRPYIVQ
     EVIYGAGEPI RPEEYTGNGD VHEFRYGKDL ARVFRSERLA YLRNFGEGWG HLPSGVSSVF
     IDNHDTQRDD GGVLTYRDRG IYALANAFML AWPYGSPTVM SSYTYSSRDA GPPSDSSNKT
     RNTVCYSGWE CEHRWPVIAN MVGFRNATEG TGVSNWYDNG YQHIAFSRTG KGFITINDED
     FAVNSRSYYT GLPAGRYCDV IHGTFSAGTC SGPVITVDTN GWFTANVPAH DAIAIHLSAR
     LP
//
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