CDGT_BREBE
ID CDGT_BREBE Reviewed; 692 AA.
AC O30565;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Brevibacillus brevis (Bacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1393;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CD162;
RX PubMed=9682490; DOI=10.1111/j.1574-6968.1998.tb13117.x;
RA Kim M.H., Sohn C.B., Oh T.K.;
RT "Cloning and sequencing of a cyclodextrin glycosyltransferase gene from
RT Brevibacillus brevis CD162 and its expression in Escherichia coli.";
RL FEMS Microbiol. Lett. 164:411-418(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; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF011388; AAB65420.1; -; Genomic_DNA.
DR AlphaFoldDB; O30565; -.
DR SMR; O30565; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; O30565; -.
DR BRENDA; 2.4.1.19; 638.
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; 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; 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 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycosyltransferase; Metal-binding; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..692
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001429"
FT DOMAIN 509..587
FT /note="IPT/TIG"
FT DOMAIN 588..692
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 241
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 340
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 59..66
FT /evidence="ECO:0000250"
SQ SEQUENCE 692 AA; 77405 MW; 8CF5AD8CB9EFF57E CRC64;
MITPSFIISS FLSLPTVVEA SVTNKVNYSK DVIYQIVTDR FSDGNPANNP SGAIFSQNCS
DLHKYCGGDW QGIINKMNDG YLTDLGITAL WISQPVENVY ALHPSGYTSY HGYWARDYKK
TNPYFGNFSD FDRLVSTAHN KGIKIIMDFT PNHSSLALET NPNYVENGAL YNNGALLGNY
SNDRNKLFHH NGGTDFSSYE DSIYRNLYDL ADYDLNNKVV DQYLKESIKL WLIKIDGIRV
DAVKHMSEGW QTSLMSDIYT YKPVFTFGEW FLGTGEVDPQ NHHFANESGM SLLDFQFGQT
IRSVLKDRTS NWYDFNEMIK STEKDYDEVI DQVTFIDNHD MSRFSMVVFN FQTDIALAVL
LTSRGVPTIY YGTEQYLTGG NDPDNRKPMK TFDRSTNSYK ITSKLASLRQ RNSALGYGNT
TERWINSDVY IYERKFGNSI VLTAVNSSNR NQTISNLNTS LPQGNYTDEL QQLLDGNTIT
VNANGSANSP QLQANSVAVW QVTKESTSPL IGHVGPMIGK TGNTVTVSGE GFGDKKGSVL
FGSTSAEIVS WSNTEIQVKV PNVTAGHYNL SVVNATNTKS PAYEKFEVLS GNQVSVRFAV
NNATTNSGTN VYIVGNVSEL GNWDPNKAIG PMFNQVMYKY PTWYYDISVP AGKNLEYKYI
KKDHNGNVTW QSGNNRTYTS PATGTDTVIS NW
