ID A0A0V0TUB3_9BILA Unreviewed; 744 AA.
AC A0A0V0TUB3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 28.
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=amy {ECO:0000313|EMBL:KRX42613.1};
GN ORFNames=T05_9613 {ECO:0000313|EMBL:KRX42613.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42613.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX42613.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX42613.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX42613.1}.
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DR EMBL; JYDJ01000140; KRX42613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TUB3; -.
DR STRING; 144512.A0A0V0TUB3; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
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:UP000055048}.
FT DOMAIN 70..448
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 457..544
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 744 AA; 86580 MW; D88B295871DD7854 CRC64;
MIFQIKYFNN VYLCAFVTIY RQAIQHKIYR KMNVKPACEF PLFIFSTAFF YSYAFNSECF
KQLAVDPTRQ LVVHLFEWGW TDIAKECKNY LWKSGIGAVQ VSPPNEHIII VENNDLPWWS
RYQPISYQLY SRSGSEKEFI NMVEECNKYG IRIIADIVIN HMVGANMEGY GWHGSYFKST
PFEEYFPSVP YNETDFHDKI CNGNIEDYGN RWQVRNCRLV NLVDLDHSNP NVQASIVAYM
NRLIDIGVAG FRIDAAKHMW PDMLRKIIYQ LKPLNSAYFP KNQCPFIFNE VIDQGGEPIK
AEEYLDIGRV TNFKYGLDLS AAVRRRKNFK HLINFGEAWN YFPSNGALVF VDNHDNQRGH
GGGGPVLTFK NGNAYKMAVH FMLAWSYGLP RLMSSYYFNT ANQGPPSTGF PFFNTTSPMF
DRNGKCIAST GWTCEHRWPS FYQMSLFHQN TSNKAIWNTV VDEHRIAFSK GNSGFFALNN
HPTENWILHV NTGLPPGYYC DHITGNLNVK RNSCSGKTVF VNPNGWIDLL VRAEETLAIS
SKNALSKFEP SYRRTLVFVK KKTQIGEYLF MRGRRPSSDS TRWQNQWKNK YTIPIVHVAD
YDPSFTDYHQ WKQHDNMLQW SLPSSKIALK EKKPTVENLF KMGSPLIWTT DNKRSNAYNI
YNRYGAHYWM LDVMMDCSKT ENDWFEFHIV KQDGEMEKII NIKQCENAYL LLLGKKIKHH
LARCGYVNIV EYGMQNCTTD LEKI
//