ID Q47YS4_COLP3 Unreviewed; 470 AA. AC Q47YS4; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134}; DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134}; GN OrderedLocusNames=CPS_3370 {ECO:0000313|EMBL:AAZ26198.1}; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ26198.1, ECO:0000313|Proteomes:UP000000547}; RN [1] {ECO:0000313|EMBL:AAZ26198.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H {ECO:0000313|EMBL:AAZ26198.1}; RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). 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; CP000083; AAZ26198.1; -; Genomic_DNA. DR RefSeq; WP_011044132.1; NC_003910.7. DR AlphaFoldDB; Q47YS4; -. DR STRING; 167879.CPS_3370; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; cps:CPS_3370; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_029247_2_0_6; -. DR Proteomes; UP000000547; Chromosome. 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 InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. 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. 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}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..28 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 29..470 FT /note="Alpha-amylase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004234026" FT DOMAIN 29..384 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 470 AA; 52310 MW; 741D54850DF96547 CRC64; MKTTPLLKKF TQASIIASSL LFSQGSYADT ILHAFNWTYD DVATKAQEIA DLGYKKVLVS PAYKSSGDQW WARYQPQDFR VIHSPLGDTN DFKDMVNALK AKGVETYADI VFNHMANESS QRSDLNYPGT AVLATYAADS TYYNSIKLFG DLQTGSYGAN DFHPAGCITD WGNPGHVQYW RLCGGNGDVG LPDLDPNNWV VSQQQAYLQA LKAIGVTGFR VDAAKHMSNY HINAVFNNDI KNGVHVFGEI ITSGGAGDNS YDAFLAPYLN DTGHSAYDFP LFASLRGALG FGGSMNQLVD PAAYGQALTP DKAVTFSITH DIPTNEGFRY QILNATDEVL ANAYIMGRDG GTPMMYSDHN ESNDNNRWLD LYKRSDVAGM VKFHNTAQGH GMQVMSFNDC IILFKRDHIG VVGINKCDNG QDVWVNTAEH NLWWNKNYRD VVEGVDVQNI NSQWHKFYLP GRKARMWLME //