CDGT_KLEOX
ID CDGT_KLEOX Reviewed; 655 AA.
AC P08704;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M5a1;
RX PubMed=2951300; DOI=10.1016/0378-1119(86)90070-3;
RA Binder F., Huber O., Boeck A.;
RT "Cyclodextrin-glycosyltransferase from Klebsiella pneumoniae M5a1: cloning,
RT nucleotide sequence and expression.";
RL Gene 47:269-277(1986).
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 -!- 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; M15264; AAA25059.1; -; Genomic_DNA.
DR PIR; A29023; ALKBG.
DR AlphaFoldDB; P08704; -.
DR SMR; P08704; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ag:AAA25059; -.
DR BRENDA; 2.4.1.19; 2811.
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; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR031319; A-amylase_C.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF00686; CBM_20; 1.
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 PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Calcium; Glycosyltransferase; Metal-binding; Signal; Transferase.
FT SIGNAL 1..30
FT CHAIN 31..655
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001443"
FT DOMAIN 554..655
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 630..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 55
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 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217..220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 363
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 73025 MW; DB8F26332BED26A7 CRC64;
MKRNRFFNTS AAIAISIALN TFFCSMQTIA AEPEETYLDF RKETIYFLFL DRFSDGDPSN
NAGFNSATYD PNNLKKYTGG DLRGLINKLP YLKSLGVTSI WITPPIDNVN NTDAAGNTGY
HGYWGRDYFR IDEHFGNLDD FKELTSLMHS PDYNMKLVLD YAPNHSNAND ENEFGALYRD
GVFITDYPTN VAANTGWYHH NGGVTNWNDF FQVKNHNLFN LSDLNQSNTD VYQYLLDGSK
FWIDAGVDAI RIDAIKHMDK SFIQKWTSDI YDYSKSIGRE GFFFFGEWFG ASANTTTGVD
GNAIDYANTS GSALLDFGFR DTLERVLVGR SGNTMKTLNS YLIKRQTVFT SDDWQVVFMD
NHDMARIGTA LRSNATTFGP GNNETGGSQS EAFAQKRIDL GLVATMTVRG IPAIYYGTEH
YAANFTSNSF GQVGSDPYNR EKMPGFDTES EAFSIIKTLG DLRKSSPAIQ NGTYTELWVN
DDILVFERRS GNDIVIVALN RGEANTINVK NIAVPNGVYP SLIGNNSVSV ANKRTTLTLM
QNEAVVIRSQ SDDAENPTVQ SINFTCNNGY TISGQSVYII GNIPQLGGWD LTKAVKISPT
QYPQWSASLE LPSDLNVEWK CVKRNETNPT ANVEWQSGAN NQFNSNDTQT TNGSF
