ID   G0LCY3_ZOBGA            Unreviewed;       571 AA.
AC   G0LCY3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=malS {ECO:0000313|EMBL:CAZ94115.1};
GN   OrderedLocusNames=zobellia_42 {ECO:0000313|EMBL:CAZ94115.1};
OS   Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS   NCIMB 13871 / Dsij).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zobellia.
OX   NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ94115.1, ECO:0000313|Proteomes:UP000008898};
RN   [1] {ECO:0000313|Proteomes:UP000008898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC   {ECO:0000313|Proteomes:UP000008898};
RG   Genoscope - CEA;
RT   "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAZ94115.1, ECO:0000313|Proteomes:UP000008898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC   {ECO:0000313|Proteomes:UP000008898};
RX   PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA   Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT   "Characterization of the first alginolytic operons in a marine bacterium:
RT   from their emergence in marine Flavobacteriia to their independent
RT   transfers to marine Proteobacteria and human gut Bacteroides.";
RL   Environ. Microbiol. 14:2379-2394(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; FP476056; CAZ94115.1; -; Genomic_DNA.
DR   RefSeq; WP_013991428.1; NC_015844.1.
DR   AlphaFoldDB; G0LCY3; -.
DR   STRING; 63186.ZOBELLIA_42; -.
DR   KEGG; zga:ZOBELLIA_42; -.
DR   PATRIC; fig|63186.3.peg.42; -.
DR   HOGENOM; CLU_022115_0_1_10; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:CAZ94115.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:CAZ94115.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008898}.
FT   DOMAIN          56..481
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   571 AA;  65702 MW;  6F72BADB2462E85A CRC64;
     MKRLLYAVVV FSIFIACKEE RKEIIEEVPV KTDSIATHVE PVKNLPFSWE AANIYFLLTD
     RFNNGTTEND LNYDRTEPTG PLRGFMGGDI QGITQKIEEG YFSDLGINAI WFTPVVEQVH
     GSTDEGTGNT YAYHGYWTKD WTALDPNFGT RKDLEKMVKA AHKHGIRVLM DVVLNHTGPV
     TDKDEAWPEE WIRTSPTCDF TSYETTVECT LVENLPDVRT ESNEAVELPD ALLAKWKEEG
     RLSQELDELQ LFFERTGYPR APRYYIIKWL TDYVNHLGID GFRVDTVKHV NENAWSELYK
     EASFAFENWK KMHPDKVLDD QPFYMVGEVY NYGISNGREF DFKDKKVDYF AHGFKSLINF
     ELKEDAKKDY ESIFRKYDKI LRSQLNGKSV VNYLTSHDDG HPYDIERKDP IRAANILMLT
     PGASQIYYGD ETARSLTVTG TEDTPVQGDA SLRSFMNWEE LDSLPKTKEI FEHWKKLGTF
     RRKHLAVGAG IHKRLGKSPY VFSRSYSEGD IKDKVVIGLD LPKGKKSLWV KGFFGDGTKL
     YDTYSDTEVV VQNGKVILEN DYNIALLEHK E
//