ID CDGT_BACLI Reviewed; 718 AA. AC P14014; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Cyclomaltodextrin glucanotransferase; DE EC=2.4.1.19; DE AltName: Full=Cyclodextrin-glycosyltransferase; DE Short=CGTase; DE Flags: Precursor; GN Name=cgtA; OS Bacillus licheniformis. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=1402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2137908; DOI=10.1093/nar/18.1.199; RA Hill D.E., Aldape R., Rozzell J.D.; RT "Nucleotide sequence of a cyclodextrin glucosyltransferase gene, cgtA, from RT Bacillus licheniformis."; RL Nucleic Acids Res. 18:199-199(1990). CC -!- CATALYTIC ACTIVITY: CC Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of CC a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- DOMAIN: May consist of two protein domains: the one in the N-terminal CC side cleaves the alpha-1,4-glucosidic bond in starch, and the other in CC the C-terminal side catalyzes other activities, including the CC reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the CC maltooligosaccharide produced. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. 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; X15752; CAA33763.1; -; Genomic_DNA. DR PIR; S15920; ALBSMX. DR AlphaFoldDB; P14014; -. DR SMR; P14014; -. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR BRENDA; 2.4.1.19; 669. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0043895; F:cyclomaltodextrin glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11320; AmyAc_AmyMalt_CGTase_like; 1. DR CDD; cd00604; IPT_CGTD; 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; 2. 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; CBM20. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF00686; CBM_20; 1. DR Pfam; PF01833; TIG; 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; SSF81296; E set domains; 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; Disulfide bond; Glycosyltransferase; Metal-binding; Secreted; KW Signal; Transferase. FT SIGNAL 1..34 FT /evidence="ECO:0000250" FT CHAIN 35..718 FT /note="Cyclomaltodextrin glucanotransferase" FT /id="PRO_0000001432" FT DOMAIN 532..612 FT /note="IPT/TIG" FT DOMAIN 613..718 FT /note="CBM20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594" FT REGION 35..172 FT /note="A1" FT REGION 173..236 FT /note="B" FT REGION 237..440 FT /note="A2" FT REGION 441..528 FT /note="C" FT REGION 529..614 FT /note="D" FT REGION 615..718 FT /note="E" FT ACT_SITE 263 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 291 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 134..135 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 227..230 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 233 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 261 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 266..267 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 267 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 405 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 409 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 362 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT DISULFID 77..84 FT /evidence="ECO:0000250" SQ SEQUENCE 718 AA; 78003 MW; B3CDE14A81D5DC4E CRC64; MFQMAKRVLL STTLTFSLLA GSALPFLPAS AIYADADTAV TNKQNFSTDV IYQVFTDRFL DGNPSNNPTG AAFDGTCSNL KLYCGGDWQG LVNKINDNYF SDLGVTALWI SQPVENIFAT INYSGVTNTA YHGYWARDFK KTNPYFGTMT DFQNLVTTAH AKGIKIIIDF APNHTSPAME TDTSFAENGK LYDNGNLVGG YTNDTNGYFH HNGGSDFSTL ENGIYKNLYD LADLNHNNST IDTYFKDAIK LWLDMGVDGI RVDAVKHMPQ GWQKNWMSSI YAHKPVFTFG EWFLGSAAPD ADNTDFANES GMSLLDFRFN SAVRNVFRDN TSNMYALDSM LTATAADYNQ VNDQVTFIDN HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRG KMPSFSKSTT AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYIYERKFG KSVAVVAVNR NLTTPTSITN LNTSLPSGTY TDVLGGVLNG NNITSSGGNI SSFTLAAGAT AVWQYTASET TPTIGHVGPV MGKPGNVVTI DGRGFGSAKG TVYFGTTAVT GSAITSWEDT QIKVTIPPVA GGDYAVKVAA NGVNSNAYND FTILSGDQVS VRFVINNATT ALGENIYLTG NVSELGNWTT GAASIGPAFN QVIHAYPTWY YDVSVPAGKQ LEFKFFKKNG ATITWEGGSN HTFTTPTSGT ATVTINWQ //