CDGT_BACS0
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 03-AUG-2022, entry version 137.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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}.
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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 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; -.
DR AlphaFoldDB; 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: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; 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..320
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 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
