ID A0A0V0ZVI0_9BILA Unreviewed; 739 AA.
AC A0A0V0ZVI0;
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=Amy2 {ECO:0000313|EMBL:KRY16138.1};
GN ORFNames=T12_14692 {ECO:0000313|EMBL:KRY16138.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY16138.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY16138.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY16138.1};
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:KRY16138.1}.
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DR EMBL; JYDQ01000083; KRY16138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZVI0; -.
DR STRING; 990121.A0A0V0ZVI0; -.
DR Proteomes; UP000054783; 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:UP000054783}.
FT DOMAIN 76..454
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 462..548
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 739 AA; 83453 MW; FD91E6CE37175802 CRC64;
MGRQHTGKDV KKKQLVNQDV YLDQILLLFF AYSMQKHFTR LIAWLLLVVH WQVVIGAGDK
VSDDCFDELQ TDLHRPVAVH LFEWKWTDIA NECETFLKDT GIGLIQVSPP NEHAVFEHEG
DYSWWLRYQP VSYLLHSRSG TEKEFIDMVQ RCMKVGIKIL VDGVINHMVG ANMKGYGSGG
SYYNSTPFKE SFPAVPYGPS DFNDDICNDN IQNYGNAAEV RNCRLVSLID LKLSKVEVQQ
KIADYLNHLI DIGVAGFRID AAKHMWPDDI RNILQRVKHL NPAYYPKDKC AFVFHEVIDQ
GAEAIQGSEY VDFGRITNFR YGLDLSAAVM RNKNFLYFKN FGPEWNYWEN HDVLVFVDNH
DNQRGSGGGG KVLTYKTPKM YKLAVSFMLA WNYGIPRLMS SYYFDGHDMG PPSSGKPDFK
TKSPTFTPDG LCNKSSGWVC EHRWHEIKRM TLFSASVAGL PNTNIISDHH RIAFSRGSNG
FYALNNDPHN SWVVQVQTSL PAGFYCDFMT GSVTSKGCSG KTIEVTTDGK VKLVVEPETA
VAISVASKLT LPPSYKRTVV LIHFPTTKGQ NVFIRGGVHS SHRKGCKADV IDTPCSIPII
HIEDVQSSWE EFIDWRSDDY FLDWSTGDNA EGSSTTGTPL AWSTNIKNQA GYQWLNKYGE
HYWLMDVLMD CNRTESGWFE FQSAMDSSNL VESAIKQTKC NGDGGVAEPP FTTTFHAARC
GFVNVFQFNT PACTIESIK
//
