ID CDGT2_NIACI Reviewed; 713 AA. AC P43379; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 03-MAY-2023, entry version 134. 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 Niallia circulans (Bacillus circulans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia. OX NCBI_TaxID=1397; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37, AND X-RAY RP CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=251; RX PubMed=8107143; DOI=10.1006/jmbi.1994.1168; RA Lawson C.L., van Montfort R., Strokopytov B., Rozeboom H.J., Kalk K.H., RA de Vries G.E., Penninga D., Dijkhuizen L., Dijkstra B.W.; RT "Nucleotide sequence and X-ray structure of cyclodextrin RT glycosyltransferase from Bacillus circulans strain 251 in a maltose- RT dependent crystal form."; RL J. Mol. Biol. 236:590-600(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-713 IN COMPLEX WITH ACARBOSE. RX PubMed=7857935; DOI=10.1021/bi00007a018; RA Strokopytov B., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., RA Dijkstra B.W.; RT "X-ray structure of cyclodextrin glycosyltransferase complexed with RT acarbose. Implications for the catalytic mechanism of glycosidases."; RL Biochemistry 34:2234-2240(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-256/GLN-284, ACTIVE RP SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-256; GLU-284 AND ASP-355. RC STRAIN=251; RX PubMed=7493956; DOI=10.1074/jbc.270.49.29256; RA Knegtel R.M.A., Strokopytov B., Penninga D., Faber O.G., Rozeboom H.J., RA Kalk K.H., Dijkhuizen L., Dijkstra B.W.; RT "Crystallographic studies of the interaction of cyclodextrin RT glycosyltransferase from Bacillus circulans strain 251 with natural RT substrates and products."; RL J. Biol. Chem. 270:29256-29264(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=8955113; DOI=10.1074/jbc.271.51.32777; RA Penninga D., van der Veen B.A., Knegtel R.M.A., van Hijum S.A.F.T., RA Rozeboom H.J., Kalk K.H., Dijkstra B.W., Dijkhuizen L.; RT "The raw starch binding domain of cyclodextrin glycosyltransferase from RT Bacillus circulans strain 251."; RL J. Biol. Chem. 271:32777-32784(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR. RC STRAIN=251; RX PubMed=8672460; DOI=10.1021/bi952339h; RA Strokopytov B., Knegtel R.M.A., Penninga D., Rozeboom H.J., Kalk K.H., RA Dijkhuizen L., Dijkstra B.W.; RT "Structure of cyclodextrin glycosyltransferase complexed with a RT maltononaose inhibitor at 2.6-A resolution. Implications for product RT specificity."; RL Biochemistry 35:4241-4249(1996). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 28-713 OF MUTANT ASN-256/GLN-284 RP IN COMPLEXES WITH CALCIUM IONS AND MALTOTETRAOSE, ACTIVE SITE, AND RP DISULFIDE BOND. RX PubMed=10331869; DOI=10.1038/8235; RA Uitdehaag J.C., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., RA Withers S.G., Dijkstra B.W.; RT "X-ray structures along the reaction pathway of cyclodextrin RT glycosyltransferase elucidate catalysis in the alpha-amylase family."; RL Nat. Struct. Biol. 6:432-436(1999). 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 Evidence={ECO:0000269|PubMed:7493956}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 3 Ca(2+) ions per subunit.; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7857935}. 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; X78145; CAA55023.1; -; Genomic_DNA. DR PIR; A58800; A58800. DR PDB; 1CDG; X-ray; 2.00 A; A=28-713. DR PDB; 1CGV; X-ray; 2.50 A; A=28-713. DR PDB; 1CGW; X-ray; 2.50 A; A=28-713. DR PDB; 1CGX; X-ray; 2.50 A; A=28-713. DR PDB; 1CGY; X-ray; 2.50 A; A=28-713. DR PDB; 1CXE; X-ray; 2.10 A; A=28-713. DR PDB; 1CXF; X-ray; 2.10 A; A=28-713. DR PDB; 1CXH; X-ray; 2.41 A; A=28-713. DR PDB; 1CXI; X-ray; 2.20 A; A=28-713. DR PDB; 1CXK; X-ray; 2.09 A; A=28-713. DR PDB; 1CXL; X-ray; 1.81 A; A=28-713. DR PDB; 1D3C; X-ray; 1.78 A; A=28-713. DR PDB; 1DTU; X-ray; 2.40 A; A=28-713. DR PDB; 1EO5; X-ray; 2.00 A; A=28-713. DR PDB; 1EO7; X-ray; 2.48 A; A=28-713. DR PDB; 1KCK; X-ray; 2.43 A; A=28-713. DR PDB; 1KCL; X-ray; 1.94 A; A=28-713. DR PDB; 1OT1; X-ray; 2.00 A; A=28-713. DR PDB; 1OT2; X-ray; 2.10 A; A=28-713. DR PDB; 1PEZ; X-ray; 2.32 A; A=28-713. DR PDB; 1PJ9; X-ray; 2.00 A; A=28-713. DR PDB; 1TCM; X-ray; 2.20 A; A/B=28-713. DR PDB; 2CXG; X-ray; 2.50 A; A=28-713. DR PDB; 2DIJ; X-ray; 2.60 A; A=28-713. DR PDBsum; 1CDG; -. DR PDBsum; 1CGV; -. DR PDBsum; 1CGW; -. DR PDBsum; 1CGX; -. DR PDBsum; 1CGY; -. DR PDBsum; 1CXE; -. DR PDBsum; 1CXF; -. DR PDBsum; 1CXH; -. DR PDBsum; 1CXI; -. DR PDBsum; 1CXK; -. DR PDBsum; 1CXL; -. DR PDBsum; 1D3C; -. DR PDBsum; 1DTU; -. DR PDBsum; 1EO5; -. DR PDBsum; 1EO7; -. DR PDBsum; 1KCK; -. DR PDBsum; 1KCL; -. DR PDBsum; 1OT1; -. DR PDBsum; 1OT2; -. DR PDBsum; 1PEZ; -. DR PDBsum; 1PJ9; -. DR PDBsum; 1TCM; -. DR PDBsum; 2CXG; -. DR PDBsum; 2DIJ; -. DR AlphaFoldDB; P43379; -. DR SMR; P43379; -. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR BRENDA; 2.4.1.19; 649. DR SABIO-RK; P43379; -. DR EvolutionaryTrace; P43379; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. DR GO; GO:0043895; F:cyclomaltodextrin glucanotransferase activity; IEA:UniProtKB-EC. 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; 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; 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 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 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Glycosyltransferase; Metal-binding; Secreted; Signal; Transferase. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:8107143" FT CHAIN 28..713 FT /note="Cyclomaltodextrin glucanotransferase" FT /id="PRO_0000001431" 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 BINDING 172..174 FT /ligand="substrate" 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 BINDING 259..260 FT /ligand="substrate" FT BINDING 260 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 342 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT BINDING 354 FT /ligand="substrate" FT BINDING 398 FT /ligand="substrate" FT BINDING 402 FT /ligand="substrate" FT BINDING 604 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT SITE 355 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT DISULFID 70..77 FT /evidence="ECO:0000269|PubMed:10331869" FT MUTAGEN 256 FT /note="D->N: Reduces activity 23000-fold. Reduces activity FT 520000-fold; when associated with N-355." FT /evidence="ECO:0000269|PubMed:7493956" FT MUTAGEN 284 FT /note="E->Q: Reduces activity 4100-fold." FT /evidence="ECO:0000269|PubMed:7493956" FT MUTAGEN 355 FT /note="D->N: Reduces activity 56000-fold. Reduces activity FT 520000-fold; when associated with N-256." FT /evidence="ECO:0000269|PubMed:7493956" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 81..89 FT /evidence="ECO:0007829|PDB:1D3C" FT TURN 90..97 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1CXL" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:1TCM" FT STRAND 128..135 FT /evidence="ECO:0007829|PDB:1D3C" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 142..154 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1D3C" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 232..247 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 263..274 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 303..308 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 310..320 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 327..340 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:1KCL" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:1OT1" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:1TCM" FT HELIX 366..377 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 379..386 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 413..421 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 429..433 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 443..451 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 453..462 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:1EO7" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:1D3C" FT TURN 486..491 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 500..502 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 514..520 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 527..532 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 534..536 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 555..558 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 568..571 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 573..579 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 585..593 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 603..608 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 610..621 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 630..637 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 638..640 FT /evidence="ECO:0007829|PDB:1D3C" FT TURN 641..643 FT /evidence="ECO:0007829|PDB:1D3C" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 655..658 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 663..670 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 674..683 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 686..689 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:1TCM" FT STRAND 695..698 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 701..703 FT /evidence="ECO:0007829|PDB:1D3C" FT STRAND 705..710 FT /evidence="ECO:0007829|PDB:1D3C" SQ SEQUENCE 713 AA; 77309 MW; 8ABBFB2C633A004B CRC64; MKKFLKSTAA LALGLSLTFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YSIINYSGVN NTAYHGYWAR DFKKTNPAYG TIADFQNLIA AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE NGRLYDNGTL LGGYTNDTQN LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDVYLKD AIKMWLDLGI DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVSPENHKFA NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF IDNHDMERFH ASNANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGTDPD NRARIPSFST STTAYQVIQK LAPLRKCNPA IAYGSTQERW INNDVLIYER KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ GSYNDVLGGL LNGNTLSVGS GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV TITIDGRGFG SSKGTVYFGT TAVSGADITS WEDTQIKVKI PAVAGGNYNI KVANAAGTAS NVYDNFEVLS GDQVSVRFVV NNATTALGQN VYLTGSVSEL GNWDPAKAIG PMYNQVVYQY PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP SSGTATINVN WQP //