ID B7VQR3_VIBA3 Unreviewed; 456 AA. AC B7VQR3; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134}; DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134}; GN OrderedLocusNames=VS_II0295 {ECO:0000313|EMBL:CAV25697.1}; OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV25697.1, ECO:0000313|Proteomes:UP000009100}; RN [1] {ECO:0000313|EMBL:CAV25697.1, ECO:0000313|Proteomes:UP000009100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32 {ECO:0000313|EMBL:CAV25697.1, RC ECO:0000313|Proteomes:UP000009100}; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) 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|RuleBase:RU361134}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FM954973; CAV25697.1; -; Genomic_DNA. DR AlphaFoldDB; B7VQR3; -. DR STRING; 575788.VS_II0295; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; vsp:VS_II0295; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_029247_2_0_6; -. DR Proteomes; UP000009100; Chromosome 2. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd11315; AmyAc_bac1_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. 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 PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}. FT DOMAIN 8..378 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 456 AA; 51676 MW; CC020705EE66C492 CRC64; MLSTPATDVI LHAFDWCYAD VMKNAPLIQE LGYKSVLVSP AMKSLRGPKG CDRDTGTQWW QRYQPQDYRV IDNQLGDTQD FTAMVNTLKQ HGLRTYVDVV FNHMANESSI RGDLTYPNQQ DMASYQQDSE YYESVRLFGD LSKPLFDEND FVEAFGIKNW KDTWEVQNGR ITGGASDPGL PTLLDNDNVV TQQRAYLKAL KVIGVKGFRI DAAKHMTLSH LRKVWTDDIC EEMHIFGEII TDGGATKEEY ELFLEPYLKH TRLGAYDFPL FNTIFKAFEE QGSFKSLINP YCFGQALSNM RAITFAVTHD IPNNEVFLEH VMDEVDEQLA HAFILGRDGG VPLVYSELST SGILDKSGQP RWLNDWQAPY MKNMIQFHNH VHGEAMQVVE ANDDLLVFVR GDKGIVVINK SKRSKTASLN WTGAVTDLLS GEVFECVGKD LTIKVESNQC MMLTTN //