ID K1QDY3_CRAGI Unreviewed; 520 AA.
AC K1QDY3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=CGI_10022189 {ECO:0000313|EMBL:EKC32158.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC32158.1};
RN [1] {ECO:0000313|EMBL:EKC32158.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC32158.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(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|ARBA:ARBA00000548,
CC ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; JH815938; EKC32158.1; -; Genomic_DNA.
DR RefSeq; XP_011448249.1; XM_011449947.2.
DR AlphaFoldDB; K1QDY3; -.
DR GeneID; 105342874; -.
DR KEGG; crg:105342874; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; K1QDY3; -.
DR OMA; FRYAYDL; -.
DR OrthoDB; 3249969at2759; -.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 30..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 423..511
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 520 AA; 58006 MW; 5BE7CA21B9674FE7 CRC64;
MFQVLLWCPL FVGIVRGGTW SNPTCAPGRH TITHLFEWKW SDIAAECERF LGPKGYCGVQ
ISPPSENRIV TNPNRPWEER YQPVSYKLVT RSGNEADLRD MIQRCNKVNV RIYADVVFNH
MTGSGASGTG TGGSHWDSGT LSYPGVPFSA WDFNGGTECS TGDGGIHNYN DPNEVRNCRL
LGMADLKLSK DYVRDTVAGY LNHLISLGVA GFRVDAAKHM WPGDLRAVFE RLHDLNTAYF
TAGTKPFIYL EVIDLGNEPI KAAEYTGIAR VTDFIYGIKI AEVFRHHNQA KWLRTWGDHW
GMPNSNDAVV FIDNHDTQRG HSGEGGVLTF YEPRSYKMAT EFMLAHPYGF TRVMSSYRWN
RDFHDGRDHN SWMGPPHNGD MSIKSPSIQP DMSCGNGWIC EHRWRQIYNM VAFRNVVMGT
TLTNWWDNGD YAIAFSRGNK GFIVINAGTS DINVNLQTGL SQGTYCDVIS GNYENGSCTG
NEVHVGGDGH AHFHISSGIE DPVIAIHIGA KKGSTKKVTT
//
