CDGT_BACOH
ID CDGT_BACOH Reviewed; 704 AA.
AC P27036;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 ohbensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1481;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1368710; DOI=10.1007/bf00169623;
RA Sin K.A., Nakamura A., Kobayashi K., Masaki H., Uozumi T.;
RT "Cloning and sequencing of a cyclodextrin glucanotransferase gene from
RT Bacillus ohbensis and its expression in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 35:600-605(1991).
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; D90243; BAA14289.2; -; Genomic_DNA.
DR PIR; I39805; I39805.
DR AlphaFoldDB; P27036; -.
DR SMR; P27036; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 679.
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..29
FT CHAIN 30..704
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001436"
FT DOMAIN 520..598
FT /note="IPT/TIG"
FT DOMAIN 599..704
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
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 122..123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
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 215..218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 350
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 68..75
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 78621 MW; 04FA14951D5ACECB CRC64;
MKNLTVLLKT IPLALLLFIL LSLPTAAQAD VTNKVNYTRD VIYQIVTDRF SDGDPSNNPT
GAIYSQDCSD LHKYCGGDWQ GIIDKINDGY LTDLGITAIW ISQPVENVYA LHPSGYTSYH
GYWARDYKRT NPFYGDFSDF DRLMDTAHSN GIKVIMDFTP NHSSPALETD PSYAENGAVY
NDGVLIGNYS NDPNNLFHHN GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKLW
LDKGIDGIRV DAVKHMSEGW QTSLMSDIYA HEPVFTFGEW FLGSGEVDPQ NHHFANESGM
SLLDFQFGQT IRDVLMDGSS NWYDFNEMIA STEEDYDEVI DQVTFIDNHD MSRFSFEQSS
NRHTDIALAV LLTSRGVPTI YYGTEQYLTG GNDPENRKPM SDFDRTTNSY QIISTLASLR
QNNPALGYGN TSERWINSDV YIYERSFGDS VVLTAVNSGD TSYTINNLNT SLPQGQYTDE
LQQLLDGNEI TVNSNGAVDS FQLSANGVSV WQITEEHASP LIGHVGPMMG KHGNTVTITG
EGFGDNEGSV LFDSDFSDVL SWSDTKIEVS VPDVTAGHYD ISVVNAGDSQ SPTYDKFEVL
TGDQVSIRFA VNNATTSLGT NLYMVGNVNE LGNWDPDQAI GPMFNQVMYQ YPTWYYDISV
PAEENLEYKF IKKDSSGNVV WESGNNHTYT TPATGTDTVL VDWQ
