CDGT2_NIACI
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-AUG-2022, entry version 130.
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; Firmicutes; 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 PRIDE; P43379; -.
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 Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 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 InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
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; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
