CDGT_BACS8
ID CDGT_BACS8 Reviewed; 713 AA.
AC P17692;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, 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 AltName: Full=Raw-starch-digesting amylase;
DE Flags: Precursor;
GN Name=cgt;
OS Bacillus sp. (strain B1018).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-47.
RX PubMed=1689153; DOI=10.1016/0006-291x(90)90855-h;
RA Itkor P., Tsukagoshi N., Udaka S.;
RT "Nucleotide sequence of the raw-starch-digesting amylase gene from Bacillus
RT sp. B1018 and its strong homology to the cyclodextrin glucanotransferase
RT genes.";
RL Biochem. Biophys. Res. Commun. 166:630-636(1990).
CC -!- FUNCTION: This endo-type adsorbable amylase is capable to digest raw
CC starch.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M33302; AAA22239.1; -; Genomic_DNA.
DR EMBL; D90112; BAA14140.1; -; Genomic_DNA.
DR PIR; S09196; S09196.
DR AlphaFoldDB; P17692; -.
DR SMR; P17692; -.
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; Glycosyltransferase; Metal-binding;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1689153"
FT CHAIN 28..713
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001433"
FT DOMAIN 526..607
FT /note="IPT/TIG"
FT DOMAIN 608..713
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
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"
SQ SEQUENCE 713 AA; 77421 MW; 85FB616DA687B888 CRC64;
MKKFLKMTAA FSLGLSLAFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN
PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YSIINYSGVN
NTAYHGYWAR DFKKTNPAYG TIADFQNLIA AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE
NGRLYDNGTL LGGYTNDTQN LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTSDVYLKD
AIKMWLDLGI DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVGPENHKFA
NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF IDNHDMERFH
ASNANRRKLE QALAFTLILA RVPAIYYGTE QYMSGGTDPD NRARIPSFST STTAYQVIQK
LAPLRKSNPA IAYGSTQERW INNDVLIYER KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ
GSYNDVLGGL LNGNTLTVGS GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV
TITIDGRGFG SSKGTVYFGT TAVSGANITS WEDTQIKVKI PAVAGGIYNI KVANAAGTAS
NVYDNFEVLS GDQVSVRFVV NNATTALGQN LYLTGNVSEL GNWDPAKAIG PMYNQVVYQY
PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP SSGTATINVN WQP
