ID   CDGT_BACS3              Reviewed;         712 AA.
AC   P09121;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   02-SEP-2026, entry version 127.
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 38-2).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=1412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-44.
RX   PubMed=2972812; DOI=10.1099/00221287-134-1-97;
RA   Kaneko T., Hamamoto T., Horikoshi K.;
RT   "Molecular cloning and nucleotide sequence of the cyclomaltodextrin
RT   glucanotransferase gene from the alkalophilic Bacillus sp. strain no.
RT   38-2.";
RL   J. Gen. Microbiol. 134:97-105(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-586.
RA   Hamamoto T., Kaneko T., Horikoshi K.;
RT   "Nucleotide sequence of the cyclomaltodextrin glucanotransferase (CGTase)
RT   gene from alkalophilic Bacillus sp. strain No. 38-2.";
RL   Agric. Biol. Chem. 51:2019-2022(1987).
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; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
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; M19880; AAA22309.1; -; Genomic_DNA.
DR   EMBL; D00129; BAA00077.1; -; Genomic_DNA.
DR   AlphaFoldDB; P09121; -.
DR   SMR; P09121; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0043895; F:cyclomaltodextrin glucanotransferase activity; IEA:UniProtKB-EC.
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; CBM20.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
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   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   Calcium; Direct protein sequencing; Disulfide bond; Glycosyltransferase;
KW   Metal-binding; Secreted; Signal; Transferase.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:2972812"
FT   CHAIN           28..712
FT                   /note="Cyclomaltodextrin glucanotransferase"
FT                   /id="PRO_0000001439"
FT   DOMAIN          526..606
FT                   /note="IPT/TIG"
FT   DOMAIN          607..712
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..608
FT                   /note="D"
FT   REGION          609..712
FT                   /note="E"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
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        70..77
FT                   /evidence="ECO:0000250"
FT   CONFLICT        582..586
FT                   /note="VPGGI -> SWRHL (in Ref. 2; BAA00077)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   712 AA;  78249 MW;  4FAA8F70BEF818F9 CRC64;
     MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN
     PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA IWISQPVENI YSVINYSGVH
     NTAYHGYWAR DFKKTNPAYG TMQDFKNLID TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE
     NGRLYDNGNL LGGYTNDTQN LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD
     AIKMWLDLGV DGIRVDAVKH MPFGWQKSFM STINNYKPVF NFGEWFLGVN EISPEYHQFA
     NESGMSLLDF PFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF IDNHDMERFH
     TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD NRARIPSFST TTTAYQVIQK
     LAPLRKSNPA IAYGSTQERW INNDVIIYER KFGNNVAVVA INRNMNTPAS ITGLVTSLPQ
     GSYNDVLGGI LNGNTLTVGA GGAASNFTLA PGGTAVWQYT TDATAPINGN VGPMMAKAGV
     TITIDGRASA RQGTVYFGTT AVTGADIVAW EDTQIQVKIL RVPGGIYDIR VANAAGAASN
     IYDNFEVLTG DQVTVRFVIN NATTALGQNV FLTGNVSELG NWDPNNAIGP MYNQVVYQYP
     TWYYDVSVPA GQTIEFKFLK KQGSTVTWEG GANRTFTTPT SGTATVNVNW QP
//