ID CDGT_BACS0 Reviewed; 713 AA. AC P05618; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 02-SEP-2026, entry version 145. DE RecName: Full=Cyclomaltodextrin glucanotransferase; DE EC=2.4.1.19; DE AltName: Full=Cyclodextrin-glycosyltransferase; DE Short=CGTase; DE Flags: Precursor; GN Name=cgt; OS Bacillus sp. (strain 1011). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=1410; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2957361; DOI=10.1128/jb.169.9.4399-4402.1987; RA Kimura K., Kataoka S., Ishii Y., Takano T., Yamane K.; RT "Nucleotide sequence of the beta-cyclodextrin glucanotransferase gene of RT alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid RT sequence to those of alpha-amylases."; RL J. Bacteriol. 169:4399-4402(1987). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-713. RX PubMed=15299574; DOI=10.1107/s0907444996008438; RA Harata K., Haga K., Nakamura A., Aoyagi M., Yamane K.; RT "X-ray structure of cyclodextrin glucanotransferase from alkalophilic RT Bacillus Sp. 1011. Comparison of two independent molecules at 1.8-A RT resolution."; RL Acta Crystallogr. D 52:1136-1145(1996). 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; CC Note=Binds 2 calcium ions per subunit.; 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; M17366; AAA22308.1; -; Genomic_DNA. DR PIR; A26678; ALBSG1. DR PDB; 1D7F; X-ray; 1.90 A; A/B=28-713. DR PDB; 1DED; X-ray; 2.00 A; A/B=28-713. DR PDB; 1I75; X-ray; 2.00 A; A/B=28-713. DR PDB; 1PAM; X-ray; 1.80 A; A/B=28-713. DR PDB; 1UKQ; X-ray; 2.00 A; A/B=28-713. DR PDB; 1UKS; X-ray; 1.90 A; A/B=28-713. DR PDB; 1UKT; X-ray; 2.20 A; A/B=28-713. DR PDB; 1V3J; X-ray; 2.00 A; A/B=28-713. DR PDB; 1V3K; X-ray; 2.00 A; A/B=28-713. DR PDB; 1V3L; X-ray; 2.10 A; A/B=28-713. DR PDB; 1V3M; X-ray; 2.00 A; A/B=28-713. DR AlphaFoldDB; P05618; -. DR MDposit; P05618; -. DR MDRepo; P05618; -. DR SMR; P05618; -. DR DrugBank; DB01841; 4,6-Dideoxyglucose. DR DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03206; Duvoglustat. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR BRENDA; 2.4.1.19; 691. DR EvolutionaryTrace; P05618; -. 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; cd05807; CBM20_CGTase; 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. DR PDBsum; 1D7F; -. DR PDBsum; 1DED; -. DR PDBsum; 1I75; -. DR PDBsum; 1PAM; -. DR PDBsum; 1UKQ; -. DR PDBsum; 1UKS; -. DR PDBsum; 1UKT; -. DR PDBsum; 1V3J; -. DR PDBsum; 1V3K; -. DR PDBsum; 1V3L; -. DR PDBsum; 1V3M; -. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Disulfide bond; Glycosyltransferase; Metal-binding; KW Secreted; Signal; Transferase. FT SIGNAL 1..27 FT CHAIN 28..713 FT /note="Cyclomaltodextrin glucanotransferase" FT /id="PRO_0000001437" FT DOMAIN 526..607 FT /note="IPT/TIG" FT DOMAIN 608..713 FT /note="CBM20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594" FT REGION 28..165 FT /note="A1" FT REGION 166..229 FT /note="B" FT REGION 230..433 FT /note="A2" FT REGION 434..522 FT /note="C" FT REGION 523..609 FT /note="D" FT REGION 610..713 FT /note="E" FT ACT_SITE 256 FT /note="Nucleophile" FT ACT_SITE 284 FT /note="Proton donor" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 80 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 127..128 FT /ligand="substrate" FT BINDING 166 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 220..223 FT /ligand="substrate" FT BINDING 226 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 259..260 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 354 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 398 FT /ligand="substrate" FT BINDING 402 FT /ligand="substrate" FT SITE 355 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT DISULFID 70..77 FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 81..89 FT /evidence="ECO:0007829|PDB:1PAM" FT TURN 90..93 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 128..135 FT /evidence="ECO:0007829|PDB:1PAM" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 142..154 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1PAM" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:1UKT" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1D7F" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 232..247 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 263..276 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 303..308 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 310..317 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 318..322 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 327..340 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:1UKT" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:1DED" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:1DED" FT HELIX 366..378 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 379..386 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 403..405 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 413..421 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 429..433 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 443..452 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 455..462 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:1V3J" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:1UKT" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:1PAM" FT TURN 486..491 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 500..502 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 514..519 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 527..532 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 534..536 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 555..558 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 568..571 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 573..579 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 585..593 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 603..608 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 610..622 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 630..637 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 638..640 FT /evidence="ECO:0007829|PDB:1PAM" FT TURN 641..643 FT /evidence="ECO:0007829|PDB:1PAM" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 655..658 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 663..670 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 673..683 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 686..689 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 695..698 FT /evidence="ECO:0007829|PDB:1PAM" FT STRAND 701..710 FT /evidence="ECO:0007829|PDB:1PAM" SQ SEQUENCE 713 AA; 78340 MW; 524B259526B56C52 CRC64; MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA IWISQPVENI YSVINYSGVN NTAYHGYWAR DFKKTNPAYG TMQDFKNLID TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE NGRLYDNGNL LGGYTNDTQN LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD AIKMWLDLGV DGIRVDAVKH MPFGWQKSFM ATINNYKPVF TFGEWFLGVN EISPEYHQFA NESGMSLLDF RFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF IDNHDMERFH TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD NRARLPSFST TTTAYQVIQK LAPLRKSNPA IAYGSTHERW INNDVIIYER KFGNNVAVVA INRNMNTPAS ITGLVTSLRR ASYNDVLGGI LNGNTLTVGA GGAASNFTLA PGGTAVWQYT TDATTPIIGN VGPMMAKPGV TITIDGRGFG SGKGTVYFGT TAVTGADIVA WEDTQIQVKI PAVPGGIYDI RVANAAGAAS NIYDNFEVLT GDQVTVRFVI NNATTALGQN VFLTGNVSEL GNWDPNNAIG PMYNQVVYQY PTWYYDVSVP AGQTIEFKFL KKQGSTVTWE GGANRTFTTP TSGTATVNVN WQP //