CDGT_GEOSE
ID CDGT_GEOSE Reviewed; 711 AA.
AC P31797;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NO. 2;
RX PubMed=1476442; DOI=10.1128/aem.58.12.4016-4025.1992;
RA Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K.,
RA Imanaka T.;
RT "Cyclization characteristics of cyclodextrin glucanotransferase are
RT conferred by the NH2-terminal region of the enzyme.";
RL Appl. Environ. Microbiol. 58:4016-4025(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-41.
RA Sugimoto T., Kubota M., Sakai S.;
RT "Polypeptide possessing cyclomaltodextrin glucanotransferase activity.";
RL Patent number GB2169902, 23-JUL-1986.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS.
RA Kubota M., Matsuura Y., Sakai S., Katsube Y.;
RL Submitted (FEB-1993) to the PDB data bank.
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. {ECO:0000269|Ref.3}.
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; X59042; CAA41770.1; -; Genomic_DNA.
DR EMBL; X59043; CAA41771.1; -; Genomic_DNA.
DR EMBL; X59044; CAA41772.1; -; Genomic_DNA.
DR PIR; S26588; ALBSXF.
DR PDB; 1CYG; X-ray; 2.50 A; A=32-711.
DR PDBsum; 1CYG; -.
DR AlphaFoldDB; P31797; -.
DR SMR; P31797; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P31797; -.
DR BRENDA; 2.4.1.19; 623.
DR EvolutionaryTrace; P31797; -.
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..31
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 32..711
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001442"
FT DOMAIN 526..604
FT /note="IPT/TIG"
FT DOMAIN 605..711
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 32..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..606
FT /note="D"
FT REGION 607..711
FT /note="E"
FT ACT_SITE 256
FT /note="Nucleophile"
FT ACT_SITE 284
FT /note="Proton donor"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 57
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 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 127..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 355
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 71..78
FT CONFLICT 460
FT /note="A -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1CYG"
FT TURN 93..98
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1CYG"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1CYG"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:1CYG"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:1CYG"
FT TURN 486..491
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 582..590
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 600..605
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 610..619
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 627..634
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:1CYG"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 671..679
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:1CYG"
FT STRAND 703..708
FT /evidence="ECO:0007829|PDB:1CYG"
SQ SEQUENCE 711 AA; 78923 MW; 5F9F71FF01C2CC60 CRC64;
MRRWLSLVLS MSFVFSAIFI VSDTQKVTVE AAGNLNKVNF TSDVVYQIVV DRFVDGNTSN
NPSGALFSSG CTNLRKYCGG DWQGIINKIN DGYLTDMGVT AIWISQPVEN VFSVMNDASG
SASYHGYWAR DFKKPNPFFG TLSDFQRLVD AAHAKGIKVI IDFAPNHTSP ASETNPSYME
NGRLYDNGTL LGGYTNDANM YFHHNGGTTF SSLEDGIYRN LFDLADLNHQ NPVIDRYLKD
AVKMWIDMGI DGIRMDAVKH MPFGWQKSLM DEIDNYRPVF TFGEWFLSEN EVDANNHYFA
NESGMSLLDF RFGQKLRQVL RNNSDNWYGF NQMIQDTASA YDEVLDQVTF IDNHDMDRFM
IDGGDPRKVD MALAVLLTSR GVPNIYYGTE QYMTGNGDPN NRKMMSSFNK NTRAYQVIQK
LSSLRRNNPA LAYGDTEQRW INGDVYVYER QFGKDVVLVA VNRSSSSNYS ITGLFTALPA
GTYTDQLGGL LDGNTIQVGS NGSVNAFDLG PGEVGVWAYS ATESTPIIGH VGPMMGQVGH
QVTIDGEGFG TNTGTVKFGT TAANVVSWSN NQIVVAVPNV SPGKYNITVQ SSSGQTSAAY
DNFEVLTNDQ VSVRFVVNNA TTNLGQNIYI VGNVYELGNW DTSKAIGPMF NQVVYSYPTW
YIDVSVPEGK TIEFKFIKKD SQGNVTWESG SNHVYTTPTN TTGKIIVDWQ N
