CDGT1_PAEMA
ID CDGT1_PAEMA Reviewed; 714 AA.
AC P04830;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cyclomaltodextrin glucanotransferase;
DE EC=2.4.1.19;
DE AltName: Full=Cyclodextrin-glycosyltransferase;
DE Short=CGTase;
DE Flags: Precursor;
GN Name=cgtM;
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7069 / DSM 1574 / IAM 1243 / JCM 20125 / NBRC 3490 / NRRL
RC B-388;
RX PubMed=1476442; DOI=10.1128/aem.58.12.4016-4025.1992;
RA Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K.,
RA Imanaka T.;
RT "Cyclization characteristics of cyclodextrin glucanotransferase are
RT conferred by the NH2-terminal region of the enzyme.";
RL Appl. Environ. Microbiol. 58:4016-4025(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7069 / DSM 1574 / IAM 1243 / JCM 20125 / NBRC 3490 / NRRL
RC B-388;
RX PubMed=3011735; DOI=10.1128/jb.166.3.1118-1122.1986;
RA Takano T., Fukuda M., Monma M., Kobayashi S., Kainuma K., Yamane K.;
RT "Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus
RT subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase
RT gene.";
RL J. Bacteriol. 166:1118-1122(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 -!- 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; X59045; CAA41773.1; -; Genomic_DNA.
DR EMBL; M12777; AAA22298.1; -; Genomic_DNA.
DR PIR; S31281; ALBSGR.
DR PDB; 3WMS; X-ray; 2.30 A; A=28-714.
DR PDB; 4JCL; X-ray; 1.70 A; A=28-714.
DR PDB; 6AIJ; X-ray; 2.10 A; A=27-714.
DR PDB; 6L2H; X-ray; 2.10 A; A=28-714.
DR PDBsum; 3WMS; -.
DR PDBsum; 4JCL; -.
DR PDBsum; 6AIJ; -.
DR PDBsum; 6L2H; -.
DR AlphaFoldDB; P04830; -.
DR SMR; P04830; -.
DR STRING; 44252.DJ90_1132; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 670.
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 3D-structure; Calcium; Glycosyltransferase; Metal-binding; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..27
FT CHAIN 28..714
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001434"
FT DOMAIN 527..607
FT /note="IPT/TIG"
FT DOMAIN 609..714
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..434
FT /note="A2"
FT REGION 435..523
FT /note="C"
FT REGION 524..610
FT /note="D"
FT REGION 611..714
FT /note="E"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 285
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 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 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 152..174
FT /note="AHAHNIKVVIDFAPNHTSPADRD -> LTLITSRSDRLRPQPHVSGRAGT
FT (in Ref. 2; AAA22298)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..184
FT /note="GM -> AL (in Ref. 2; AAA22298)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="HM -> QY (in Ref. 2; AAA22298)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="S -> T (in Ref. 2; AAA22298)"
FT /evidence="ECO:0000305"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4JCL"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4JCL"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6AIJ"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3WMS"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 444..453
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6AIJ"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:4JCL"
FT TURN 487..492
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 528..537
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 586..594
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 611..623
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 631..638
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:4JCL"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:4JCL"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 664..671
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 675..684
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:3WMS"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:4JCL"
FT STRAND 702..711
FT /evidence="ECO:0007829|PDB:4JCL"
SQ SEQUENCE 714 AA; 76960 MW; F8A9AE794D2F3054 CRC64;
MKSRYKRLTS LALSLSMALG ISLPAWASPD TSVDNKVNFS TDVIYQIVTD RFADGDRTNN
PAGDAFSGDR SNLKLYFGGD WQGIIDKIND GYLTGMGVTA LWISQPVENI TSVIKYSGVN
NTSYHGYWAR DFKQTNDAFG DFADFQNLID TAHAHNIKVV IDFAPNHTSP ADRDNPGFAE
NGGMYDNGSL LGAYSNDTAG LFHHNGGTDF STIEDGIYKN LYDLADINHN NNAMDAYFKS
AIDLWLGMGV DGIRFDAVKH MPFGWQKSFV SSIYGGDHPV FTFGEWYLGA DQTDGDNIKF
ANESGMNLLD FEYAQEVREV FRDKTETMKD LYEVLASTES QYDYINNMVT FIDNHDMDRF
QVAGSGTRAT EQALALTLTS RGVPAIYYGT EQYMTGDGDP NNRAMMTSFN TGTTAYKVIQ
ALAPLRKSNP AIAYGTTTER WVNNDVLIIE RKFGSSAALV AINRNSSAAY PISGLLSSLP
AGTYSDVLNG LLNGNSITVG SGGAVTNFTL AAGGTAVWQY TAPETSPAIG NVGPTMGQPG
NIVTIDGRGF GGTAGTVYFG TTAVTGSGIV SWEDTQIKAV IPKVAAGKTG VSVKTSSGTA
SNTFKSFNVL TGDQVTVRFL VNQANTNYGT NVYLVGNAAE LGSWDPNKAI GPMYNQVIAK
YPSWYYDVSV PAGTKLDFKF IKKGGGTVTW EGGGNHTYTT PASGVGTVTV DWQN
