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Database: UniProt/TrEMBL
Entry: A0A1U7RZU6_ALLSI
LinkDB: A0A1U7RZU6_ALLSI
Original site: A0A1U7RZU6_ALLSI 
ID   A0A1U7RZU6_ALLSI        Unreviewed;       512 AA.
AC   A0A1U7RZU6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=LOC102375731 {ECO:0000313|RefSeq:XP_006032219.1,
GN   ECO:0000313|RefSeq:XP_006032220.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|RefSeq:XP_006032219.1};
RN   [1] {ECO:0000313|RefSeq:XP_006032219.1, ECO:0000313|RefSeq:XP_006032220.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2022) 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_006032219.1; XM_006032157.3.
DR   RefSeq; XP_006032220.1; XM_006032158.3.
DR   STRING; 38654.A0A1U7RZU6; -.
DR   GeneID; 102375731; -.
DR   KEGG; asn:102375731; -.
DR   eggNOG; KOG2212; Eukaryota.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000189705; 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:UP000189705};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..512
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011902133"
FT   DOMAIN          26..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   512 AA;  57748 MW;  8FD67AD45952FD69 CRC64;
     MKILLVLAAV GLCWAQYNPH TKPGRTSIVH LFEWRWADIA LECERYLAPN GFGGVQISPP
     SENIIITNPW RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVHIYV DAVVNHMCGA
     GAGSGNGGTC GSYFNAQTED FPAVPFSGWD FNDGKCKTGS GEIENYNDPY QVRDCRLVSL
     LDLALEKDYV RSKIAEYMNY LIDIGVAGFR IDASKHMWPG DMKAFLDKLK NLNTQWFSSG
     SKPFIYQEVI DLGGEPIKSS EYFGNGRVTE FKYSAKLGTV IRKWNGEKMA YLRNWGEGWG
     LMPSDKALVF VDNHDNQRGH GAGGASVLTF WDPRQYKMAT GFMLAHPYGF TRVMSSFWWP
     RDFQNGKDIN DWVGPPSFED GTTKPVTVNP DTTCGNGWVC EHRWRQIRNM VIFRNVVDGQ
     PFSNWWDNNS NQVAFGRGNK GFIVFNNDDW YMNINLNTGL PAGTYCDVIS GQKEGNHCTG
     IQVHIGADGV ANFQISNQAE DPFIAIHVDA KL
//
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