ID A0A3Q2D109_CYPVA Unreviewed; 372 AA.
AC A0A3Q2D109;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000012106.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000012106.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- 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 AlphaFoldDB; A0A3Q2D109; -.
DR Ensembl; ENSCVAT00000030192.1; ENSCVAP00000012106.1; ENSCVAG00000016013.1.
DR GeneTree; ENSGT00940000163518; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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; 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; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..372
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018589160"
FT DOMAIN 26..274
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 283..371
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 42023 MW; 436D54793EF0AB04 CRC64;
MKLVILTMLF GFGVMQHNPN FQHGRTTIVQ LFEWRWSDIA AECERFLAPK GFGGIQTEQT
DQEDQRCCRG VAGHPDHRGR EEDAVQVSVH LRRAPSAKDY SYPDAPHSVI DLGGEAISYS
EYIHLGRVTE FKYGAKLGNI FRKWNEEKLF YTRTWGEGWG FMSDGNAVVF VDNHDNQRGH
GAGGSSIITF WDSKLYKMAV GYMLAHPYGV ARIMSSYRWN RNFVNGKDQN DWMGPPANTN
GSTKSVPVNS DQTCGDGWVC EHRWRQITNM VIFRNVVKQQ PQISWWDNQS NQVAFGRGDL
GFIVFNNDDW DLDVTLNTGM SGGTYCDVIS GQKDGNKCTG KQIIVSKDGN AHFKISNTDE
DPFIAIHAES KL
//
