ID CDGT1_NIACI Reviewed; 718 AA.
AC P30920;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-MAY-2023, entry version 140.
DE RecName: Full=Cyclomaltodextrin glucanotransferase;
DE EC=2.4.1.19;
DE AltName: Full=Cyclodextrin-glycosyltransferase;
DE Short=CGTase;
DE Flags: Precursor;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8;
RX PubMed=1368573; DOI=10.1007/bf00172548;
RA Nitschke L., Heeger K., Bender H., Schulz G.E.;
RT "Molecular cloning, nucleotide sequence and expression in Escherichia coli
RT of the beta-cyclodextrin glycosyltransferase gene from Bacillus circulans
RT strain no. 8.";
RL Appl. Microbiol. Biotechnol. 33:542-546(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=8;
RX PubMed=1826034; DOI=10.1016/0022-2836(91)90530-j;
RA Klein C., Schulz G.E.;
RT "Structure of cyclodextrin glycosyltransferase refined at 2.0-A
RT resolution.";
RL J. Mol. Biol. 217:737-750(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RC STRAIN=8;
RX PubMed=2531228; DOI=10.1016/0022-2836(89)90607-4;
RA Hofmann B.E., Bender H., Schulz G.E.;
RT "Three-dimensional structure of cyclodextrin glycosyltransferase from
RT Bacillus circulans at 3.4-A resolution.";
RL J. Mol. Biol. 209:793-800(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=8;
RX PubMed=9558324; DOI=10.1021/bi9729918;
RA Schmidt A.K., Cottaz S., Driguez H., Schulz G.E.;
RT "Structure of cyclodextrin glycosyltransferase complexed with a derivative
RT of its main product beta-cyclodextrin.";
RL Biochemistry 37:5909-5915(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC STRAIN=8;
RX PubMed=9738912; DOI=10.1046/j.1432-1327.1998.2550710.x;
RA Parsiegla G., Schmidt A.K., Schulz G.E.;
RT "Substrate binding to a cyclodextrin glycosyltransferase and mutations
RT increasing the gamma-cyclodextrin production.";
RL Eur. J. Biochem. 255:710-717(1998).
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; X68326; CAA48401.1; -; Genomic_DNA.
DR PIR; S23674; ALBSGC.
DR PDB; 1CGT; X-ray; 2.00 A; A=35-718.
DR PDB; 1CGU; X-ray; 2.50 A; A=35-718.
DR PDB; 3CGT; X-ray; 2.40 A; A=35-718.
DR PDB; 4CGT; X-ray; 2.60 A; A=35-718.
DR PDB; 5CGT; X-ray; 2.50 A; A=35-718.
DR PDB; 6CGT; X-ray; 2.60 A; A=35-718.
DR PDB; 7CGT; X-ray; 3.00 A; A=35-718.
DR PDB; 8CGT; X-ray; 2.40 A; A=35-718.
DR PDB; 9CGT; X-ray; 2.50 A; A=35-718.
DR PDBsum; 1CGT; -.
DR PDBsum; 1CGU; -.
DR PDBsum; 3CGT; -.
DR PDBsum; 4CGT; -.
DR PDBsum; 5CGT; -.
DR PDBsum; 6CGT; -.
DR PDBsum; 7CGT; -.
DR PDBsum; 8CGT; -.
DR PDBsum; 9CGT; -.
DR AlphaFoldDB; P30920; -.
DR SMR; P30920; -.
DR DrugBank; DB01789; 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene.
DR DrugBank; DB02469; 4,6-dideoxy-4-amino-beta-D-glucopyranoside.
DR DrugBank; DB01841; 4,6-Dideoxyglucose.
DR DrugBank; DB02670; 4-Deoxy-Alpha-D-Glucose.
DR DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol.
DR DrugBank; DB01909; Alpha-Cyclodextrin (Cyclohexa-Amylose).
DR DrugBank; DB03773; alpha-D-quinovopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03323; Maltose.
DR DrugBank; DB02394; Oxiranpseudoglucose.
DR DrugBank; DB03198; Thio-Maltohexaose.
DR DrugBank; DB01719; Thio-Maltopentaose.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 649.
DR EvolutionaryTrace; P30920; -.
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; 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 InterPro; IPR006311; TAT_signal.
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 PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Glycosyltransferase; Metal-binding;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..34
FT CHAIN 35..718
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001430"
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 BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 134..135
FT /ligand="substrate"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 174
FT /ligand="substrate"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 227..230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="substrate"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266..267
FT /ligand="substrate"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 267
FT /ligand="substrate"
FT BINDING 361
FT /ligand="substrate"
FT BINDING 405
FT /ligand="substrate"
FT BINDING 409
FT /ligand="substrate"
FT SITE 362
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 77..84
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1CGU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1CGT"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1CGT"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4CGT"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3CGT"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5CGT"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:1CGT"
FT TURN 493..498
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 591..600
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 608..613
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 615..626
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 635..642
FT /evidence="ECO:0007829|PDB:1CGT"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:1CGT"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:6CGT"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 680..691
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 701..704
FT /evidence="ECO:0007829|PDB:1CGT"
FT STRAND 707..716
FT /evidence="ECO:0007829|PDB:1CGT"
SQ SEQUENCE 718 AA; 78047 MW; E08CF0FE9C98BDA1 CRC64;
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV IYQVFTDRFL
DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF SDLGVTALWI SQPVENIFAT
INYSGVTNTA YHGYWARDFK KTNPYFGTMA DFQNLITTAH AKGIKIVIDF APNHTSPAME
TDTSFAENGR LYDNGTLVGG YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT
IDKYFKDAIK LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ VNDQVTFIDN
HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRA KMPSFSKSTT
AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYVYERKFG KSVAVVAVNR NLSTSASITG
LSTSLPTGSY TDVLGGVLNG NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV
MGKPGNVVTI DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA
SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST GSTAIGPAFN
QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN HTFTTPASGT ATVTVNWQ
//
