CDGT_BACSS
ID CDGT_BACSS Reviewed; 718 AA.
AC P31747;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 6.6.3).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=29335;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Akhmetzjanov A.A.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
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; X66106; CAA46901.1; -; Genomic_DNA.
DR PIR; S21532; ALBSG6.
DR AlphaFoldDB; P31747; -.
DR SMR; P31747; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 691.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycosyltransferase; Metal-binding; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..718
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001441"
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 /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
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 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134..135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227..230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266..267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 362
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 77..84
FT /evidence="ECO:0000250"
SQ SEQUENCE 718 AA; 78015 MW; 7644096D402707E5 CRC64;
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AAYADPDIAV TNKQSFSTDV IYQVFTDRFL
DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF SDLGVTALWI SQPVENIFAT
INYSGVTNTA YHGYWARDFK KTNPYFGTMA DFQNLITTAH AKGIKIIIDF APNHTSPAME
TDTSFAENGK LYDNGTLVGG YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT
IDKYFKDAIK LWLDMGVDGI RVDAVKHIAL GWQKSWMSSI YVHKPVFTFG EWFLGSAASD
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ VNDQVTFIDN
HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRA KMPSFSKSTT
AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYVYERKFG KSVAVVAVNR NLSTPANITG
LSTSLPTGSY TDVLGGVLNG NNITSSNGSV NSFTLAAGAT AVWQYTAAET TPTIGHVGPV
MGKPGNVVTI DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA
NGVNSNAYNH FTILTGDQVT VRFVINNAST TLGQNIYLTG NVAELGNWST GSTAIGPAFN
QVIHQYPTWY YDVSVPAGKE LEFKFFKKNG STITWEGGSN HKFTTPASGT ATVTVNWQ
