CDGT_BAC11
ID CDGT_BAC11 Reviewed; 713 AA.
AC P30921;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 17-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=72572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-44.
RX PubMed=2534600; DOI=10.1099/00221287-135-12-3447;
RA Kaneko T., Song K.B., Hamamoto T., Kudo T., Horikoshi K.;
RT "Construction of a chimeric series of Bacillus cyclomaltodextrin
RT glucanotransferases and analysis of the thermal stabilities and pH optima
RT of the enzymes.";
RL J. Gen. Microbiol. 135:3447-3457(1989).
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; M28053; AAA22310.1; -; Genomic_DNA.
DR AlphaFoldDB; P30921; -.
DR SMR; P30921; -.
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 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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycosyltransferase;
KW Metal-binding; Secreted; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2534600"
FT CHAIN 28..713
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001440"
FT DOMAIN 526..607
FT /note="IPT/TIG"
FT DOMAIN 608..713
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 28..165
FT /note="A1"
FT REGION 166..229
FT /note="B"
FT REGION 230..433
FT /note="A2"
FT REGION 434..522
FT /note="C"
FT REGION 523..609
FT /note="D"
FT REGION 610..713
FT /note="E"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Proton donor"
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 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
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 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220..223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 355
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 70..77
FT /evidence="ECO:0000250"
SQ SEQUENCE 713 AA; 77390 MW; D13AEF6C507FF45E CRC64;
MKKISKLTTA LALSLSLALS LLGPAHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN
PTGPAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YSVINYSGVN
NTAYHGYWAR DFKKTNPAYG TIADFQNLIA AAHAKNIKVI IDFAPNHTSP ASLDQPSFAE
NGKLYNNGRD EGGYTNDTHN LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDTYLKD
AIKMWLDLGI DGIRMDAVKH MPFGWQKSFM ATVNNYKPVF TFGEWFLGVN EVSAENHKFA
NVSGMSLLDF RFAQKVRQVF KDNTDNMYGL KSMLEGSATD YAQMEDQVTF IDNHDMERFH
NNSANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGNDPD NRARIPSFST TTTAYQVSKK
LAPLRKSNPA IAYGTTQERW INNDVLIYER KFGNNVAVIA VNRNVNTSAS ITGLVTSLPA
GSYTDVLGGL LNGNNLTVGS GGSASIFTLA AGGTAVWQYT TAVTAPTIGH VGPMMAKPGA
AVTIDGRGFG ATKGTVYFGT TAVTGANITA WEDTQIKVKI PAVAGGVYNI KIANSAGTSS
NVHDNFEVLS GDQVSVRFVV NNATTALGQN VYLAGSVSEL GNWDPAKAIG PLYNQVIYQY
PTWYYDVTVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP TSGTATINVN WQP
