CDGT_BACS2
ID CDGT_BACS2 Reviewed; 703 AA.
AC P31746;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 1-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=29334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-52.
RA Schmid G., Englbrecht A., Schmid D.;
RT "Cloning and nucleotide sequence of a cyclodextrin glycosyltransferase gene
RT from the alkalophilic Bacillus 1-1.";
RL (In) Huber O., Szejtli J. (eds.);
RL Proceedings of the fourth international symposium on cyclodextrins,
RL pp.71-76, Kluwer Academic Publishers, Dordrecht and Boston (1988).
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 PIR; S26399; ALBSX1.
DR AlphaFoldDB; P31746; -.
DR SMR; P31746; -.
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; 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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycosyltransferase;
KW Metal-binding; Secreted; Signal; Transferase.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 30..703
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001438"
FT DOMAIN 520..598
FT /note="IPT/TIG"
FT DOMAIN 599..703
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 30..160
FT /note="A1"
FT REGION 161..224
FT /note="B"
FT REGION 225..428
FT /note="A2"
FT REGION 429..516
FT /note="C"
FT REGION 517..600
FT /note="D"
FT REGION 601..703
FT /note="E"
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 54
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 703 AA; 78663 MW; 4D973FB21D0D9B0A CRC64;
MNDLNDFLKT ILLSFIFFLL LSLPTVAEAD VTNKVNYSKD VIYQIVTDRF SDGNPGNNPS
GAIFSQNCID LHKYCGGDWQ GIIDKINDGY LTDLGITALW ISQPVENVYA LHPSGYTSYH
GYWARDYKKT NPYYGNFDDF DRLMSTAHSN GIKVIMDFTP NHSSPALETN PNYVENGAIY
DNGALLGNYS NDQQNLFHHN GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKFW
LDKGIDGIRV DAVKHMSEGW QTSLMSEIYS HKPVFTFGEW FLGSGEVDPQ NHHFANESGM
SLLDFQFGQT IRNVLKDRTS NWYDFNEMIT STEKEYNEVI DQVTFIDNHD MSRFSVGSSS
NRQTDMALAV LLTSRGVPTI YYGTEQYVTG GNDPENRKPL KTFDRSTNSY QIISKLASLR
QTNSALGYGT TTERWLNEDI YIYERTFGNS IVLTAVNSSN SNQTITNLNT SLPQGNYTDE
LQQRLDGNTI TVNANGAVNS FQLRANSVAV WQVSNPSTSP LIGQVGPMMG KAGNTITVSG
EGFGDERGSV LFDSTSSEII SWSNTKISVK VPNVAGGYYD LSVVTAANIK SPTYKEFEVL
SGNQVSVRFG VNNATTSPGT NLYIVGNVNE LGNWDADKAI GPMFNQVMYQ YPTWYYDISV
PAGKNLEYKY IKKDQNGNVV WQSGNNRTYT SPTTGTDTVM INW
