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Database: UniProt/TrEMBL
Entry: F7ZZ17_CELGA
LinkDB: F7ZZ17_CELGA
Original site: F7ZZ17_CELGA 
ID   F7ZZ17_CELGA            Unreviewed;       609 AA.
AC   F7ZZ17;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   23-MAY-2018, entry version 47.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
DE   Flags: Precursor;
GN   OrderedLocusNames=Celgi_0766 {ECO:0000313|EMBL:AEI11285.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio
OS   gilvus).
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI11285.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D.,
RA   Brumm P., Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-2011) 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:RU003615}.
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DR   EMBL; CP002665; AEI11285.1; -; Genomic_DNA.
DR   RefSeq; WP_013882807.1; NC_015671.1.
DR   STRING; 593907.Celgi_0766; -.
DR   PRIDE; F7ZZ17; -.
DR   EnsemblBacteria; AEI11285; AEI11285; Celgi_0766.
DR   KEGG; cga:Celgi_0766; -.
DR   eggNOG; ENOG4105E54; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OMA; WKCQHAW; -.
DR   OrthoDB; POG091H0CDS; -.
DR   BioCyc; CCE593907:GH26-778-MONOMER; -.
DR   Proteomes; UP000000485; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000485};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     47       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        48    609       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003367437.
FT   DOMAIN      508    609       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   609 AA;  63625 MW;  52866964A3A593FC CRC64;
     MRTTSHPNPT AGAPDRARRR LRALAALVVG GLALAGVLSA VAPSASAAPA GSRTVGVNLF
     QWTWNSIAAE CTDHLGPDGY AWVQTSPPQE RPVLGGQWWT SYQPVSYRIE SKLGTRAEYR
     AMVDTCRAAG VQVIADVVIN HMSGQTSGTG WAGTPFSEER YPGPAGGYGP QDFHACRTNI
     ASYADRYQVQ SCRLVGLQDL DTGSDYVRQE IADYLNDLIS LGVRGFRVDA AKHIAAADLA
     AIRARLTDQS VYVVQEVIGA PGEPIQPGEY LGVGDSHEFS YARHLKSAFS GGGLASLGGL
     DSASWLLPSD KAGVFVDNHD TERNGETLSY KNGSAYRLAN VFMLAHPYGW PTVYSGYAFS
     NNDAGAPQSA NGEVDDARCG QGTFTCAHRW NETAHMVGFR NAVAGTGLVG WWADGDRLAF
     GRGDKGYVAL NRTGSPLTRT FTTSLPAGQY CDVISGGAGA TCSGTTVTVG AGGAATFTVP
     ADGAVALHVG ARPGTTTSPS PTTSPTPSPT SSAAAVAFGV SATTVWGQNI FVVGDVPALG
     GWDPARAVPL SAATYPVWRA TVSLPAGSAV QYKYVRKDAS GSVTWESGVN RTLTVPSGGT
     LSVADTWRS
//
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