CDGT_BACS3
ID CDGT_BACS3 Reviewed; 712 AA.
AC P09121;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 38-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-44.
RX PubMed=2972812; DOI=10.1099/00221287-134-1-97;
RA Kaneko T., Hamamoto T., Horikoshi K.;
RT "Molecular cloning and nucleotide sequence of the cyclomaltodextrin
RT glucanotransferase gene from the alkalophilic Bacillus sp. strain no. 38-
RT 2.";
RL J. Gen. Microbiol. 134:97-105(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-586.
RA Hamamoto T., Kaneko T., Horikoshi K.;
RT "Nucleotide sequence of the cyclomaltodextrin glucanotransferase (CGTase)
RT gene from alkalophilic Bacillus sp. strain No. 38-2.";
RL Agric. Biol. Chem. 51:2019-2022(1987).
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; M19880; AAA22309.1; -; Genomic_DNA.
DR EMBL; D00129; BAA00077.1; -; Genomic_DNA.
DR AlphaFoldDB; P09121; -.
DR SMR; P09121; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00686; CBM_20; 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:2972812"
FT CHAIN 28..712
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001439"
FT DOMAIN 526..606
FT /note="IPT/TIG"
FT DOMAIN 607..712
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..608
FT /note="D"
FT REGION 609..712
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"
FT CONFLICT 582..586
FT /note="VPGGI -> SWRHL (in Ref. 2; BAA00077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 78249 MW; 4FAA8F70BEF818F9 CRC64;
MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN
PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA IWISQPVENI YSVINYSGVH
NTAYHGYWAR DFKKTNPAYG TMQDFKNLID TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE
NGRLYDNGNL LGGYTNDTQN LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD
AIKMWLDLGV DGIRVDAVKH MPFGWQKSFM STINNYKPVF NFGEWFLGVN EISPEYHQFA
NESGMSLLDF PFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF IDNHDMERFH
TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD NRARIPSFST TTTAYQVIQK
LAPLRKSNPA IAYGSTQERW INNDVIIYER KFGNNVAVVA INRNMNTPAS ITGLVTSLPQ
GSYNDVLGGI LNGNTLTVGA GGAASNFTLA PGGTAVWQYT TDATAPINGN VGPMMAKAGV
TITIDGRASA RQGTVYFGTT AVTGADIVAW EDTQIQVKIL RVPGGIYDIR VANAAGAASN
IYDNFEVLTG DQVTVRFVIN NATTALGQNV FLTGNVSELG NWDPNNAIGP MYNQVVYQYP
TWYYDVSVPA GQTIEFKFLK KQGSTVTWEG GANRTFTTPT SGTATVNVNW QP
