ID A0A1S3HXK6_LINUN Unreviewed; 666 AA.
AC A0A1S3HXK6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 Name=LOC106158399 {ECO:0000313|RefSeq:XP_013389804.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013389804.1};
RN [1] {ECO:0000313|RefSeq:XP_013389804.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013389804.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_013389804.1; XM_013534350.1.
DR AlphaFoldDB; A0A1S3HXK6; -.
DR STRING; 7574.A0A1S3HXK6; -.
DR EnsemblMetazoa; g1339.t1; g1339.t1; g1339.
DR EnsemblMetazoa; XM_013534350.1; XP_013389804.1; LOC106158399.
DR GeneID; 106158399; -.
DR KEGG; lak:106158399; -.
DR InParanoid; A0A1S3HXK6; -.
DR OMA; WHNYKSG; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000085678; Unplaced.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 5..355
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 364..452
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_013389804.1"
SQ SEQUENCE 666 AA; 72452 MW; F6B2C214B1891783 CRC64;
LSPPSEHIVS TNPSHPWWQR YQPVSYQLNS RSGNRAAFAD MVSRCNNVGV RVYADIVVNH
MAAAGIGTGY GGSSYDSGSL SYPGVPFGPN DFNGPAECST SSGNIENYGD ANQVRNCRLL
GMPDLALGKD YVRGKVADYL NDLIGLGVAG FRIDAAKHMW PGDLAGILGR LNNLNTQWFS
SGKQPFVFHE VIDLGGEPIK GSEYKSMGRV TEFKYGKFLG KAFRGRDQLK WLETFGQSWG
MLHPFDALVF IDNHDNQRGE GGGGMDTIVT FFESRPYKMA SAFMLAHPYG LPRVMSSYHW
DRHIVGGEDH NYWIGPPHNE DWSTKDVIVN ADGTCGNGWV CEHRWRQIAN MVAFRNACDG
EEISNWWDNG NNQIAFSRGN KGFIAINNDG NGLDATLQTG LPAGLYCDVI SGDFVNRGCS
GHTISVDGSG IAHISISNSA EDPFIAIHVG AKIGENGGNE GRETQPPAPA PTPGEGWART
VVFIKKQTQY GQDLFVRGGI SHAHRTGCSQ DAATSACAIP IAYNDLGDTD HLEKFNAWRG
GDSRLDWYGP EQGQGTFGSK TASGSPTVWT TNIQGEDGYF PENRFGEHYW MLDINMDCSK
TEGGWFDIKS YLSDGSGGFW EADINQVTSC GGSAGGQAPY SSKNHVARCG YINVFEFGSG
SCIIDN
//
