ID A9WA30_CHLAA Unreviewed; 597 AA. AC A9WA30; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134}; DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134}; GN OrderedLocusNames=Caur_3528 {ECO:0000313|EMBL:ABY36712.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36712.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). 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 -!- 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; CP000909; ABY36712.1; -; Genomic_DNA. DR RefSeq; WP_012259365.1; NC_010175.1. DR RefSeq; YP_001637101.1; NC_010175.1. DR AlphaFoldDB; A9WA30; -. DR SMR; A9WA30; -. DR STRING; 324602.Caur_3528; -. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; ABY36712; ABY36712; Caur_3528. DR KEGG; cau:Caur_3528; -. DR PATRIC; fig|324602.8.peg.3975; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_013336_3_1_0; -. DR InParanoid; A9WA30; -. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR CDD; cd05808; CBM20_alpha_amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR013784; Carb-bd-like_fold. DR InterPro; IPR002044; CBM_fam20. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. 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 Pfam; PF00686; CBM_20; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SMART; SM01065; CBM_2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR SUPFAM; SSF49452; Starch-binding domain-like; 1. DR PROSITE; PS51166; CBM20; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}. FT DOMAIN 497..597 FT /note="CBM20" FT /evidence="ECO:0000259|PROSITE:PS51166" SQ SEQUENCE 597 AA; 65644 MW; 61D00CD5A01F6B19 CRC64; MPGTRFPSLR RLVLVVALLM VVSSLPFGPV HHSTARAQTS SPRTVFVHLF EWKWTDIAQE CENFLGPRGF AAVQVSPPQE HAIVAGYPWW QRYQPVSYQL TSRSGTRAEF ANMVARCKAV GVDIYVDAVI NHMTGVGSGV GSAGSTYSPY NYPGIYQYQD FHHCGRNGND DIQNYGDRYE VQNCELVNLA DLDTGSSYVR DRLAAYLNDL ISLGVAGFRI DAAKHIAAGD IAAILSRVNG SPYIYQEVIG AAGEPITPWE YTNNGDVTEF KYSNEIGRVF LNGKLAWLSQ FGEAWGMLPS DKAIVFVDNH DNQRGHGGGG TVVTYKNGVL YDLANVFMLA WPYGYPQVMS SYEFSNDFQG PPSDANGNTR SVYVNGQPNC FGEWKCEHRW RPIANMVAFR NATASTFSVS DWWSNGNNQI AFGRGDKGFV VINREDTTLN RTFQTSMAPG VYCNVIVADF TNGTCSGQTV TVDSNRRITV SIPPFSALAI HVGAKLSTQP ATVAVTFNVN ATTYWGQNVF VVGNIPQLGN WNPAQAVPLS AATYPVWSGT VNLPANTTIE YKYIKRDGSN VVWECCNNRV ITTPGSGSMT LNETWRP //