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Database: UniProt/TrEMBL
Entry: A0A1W7A9H6_9STAP
LinkDB: A0A1W7A9H6_9STAP
Original site: A0A1W7A9H6_9STAP 
ID   A0A1W7A9H6_9STAP        Unreviewed;       483 AA.
AC   A0A1W7A9H6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-SEP-2017, entry version 3.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ARQ06144.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ARQ06144.1};
GN   ORFNames=MCCS_04810 {ECO:0000313|EMBL:ARQ06144.1};
OS   Macrococcus canis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Macrococcus.
OX   NCBI_TaxID=1855823 {ECO:0000313|EMBL:ARQ06144.1, ECO:0000313|Proteomes:UP000194154};
RN   [1] {ECO:0000313|EMBL:ARQ06144.1, ECO:0000313|Proteomes:UP000194154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM45013 {ECO:0000313|EMBL:ARQ06144.1,
RC   ECO:0000313|Proteomes:UP000194154};
RX   PubMed=27902286;
RA   Gobeli Brawand S., Cotting K., Gomez-Sanz E., Collaud A., Thomann A.,
RA   Brodard I., Rodriguez Campos S., Strauss C., Perreten V.;
RT   "Macrococcus canis sp. nov., a skin bacterium associated with
RT   infections in dogs.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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DR   EMBL; CP021059; ARQ06144.1; -; Genomic_DNA.
DR   Proteomes; UP000194154; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000194154};
KW   Glycosidase {ECO:0000313|EMBL:ARQ06144.1};
KW   Hydrolase {ECO:0000313|EMBL:ARQ06144.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN        5    391       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    233    233       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    263    263       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL       104    104       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       196    196       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       204    204       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       237    237       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
SQ   SEQUENCE   483 AA;  55769 MW;  5235B575CF4048FF CRC64;
     MTKNYTMMQY FEWHANGDGA HWKRLKEDAP KLKEKGIDAI WLPPACKADH VMNTGYSIYD
     LYDLGEFDQK GQVRTKYGTK EELLDAIKAC HDNDIKVYAD IVLNHKAGAD EAETIKVVEV
     DPNDRNHVIS EPFEIDAYTK FEFPGRNNKY SDFKWNHTHF NGTDYDHKTG RSGIFKILGE
     NKDWNEFVDD EKGNFDYLMF TNIDYKHPDV REHTIEWGKW LIDTLGIDGM RMDAVKHIES
     YFIKDFSDAM REHAGEDFYF LGEYWNADLG KNQKFLEEAD YNTDLFDVKL HFNFKAASEA
     GSAYDLRTLF DDTIVAEHPE LAVTFVDNHD SQPGEALESF VKDWFKQSAY ALILLREDGY
     PCIFYGDYYG IGGDQPVEGK QLAIDPLLYI RQNKAYGEQD DYFDHPNVIG FVRRGNGNKT
     GCAVIINSSE EEAEKQMFVG KERAGEVWYD YTNTREDKIT IDEEGNGLFK VNPGSVSVYC
     EEE
//
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