CDGT_THETU
ID CDGT_THETU Reviewed; 710 AA.
AC P26827;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cyclomaltodextrin glucanotransferase;
DE EC=2.4.1.19;
DE AltName: Full=Cyclodextrin-glycosyltransferase;
DE Short=CGTase;
DE Flags: Precursor;
GN Name=amyA;
OS Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=33950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-48, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 3896 / EM1;
RX PubMed=1854207; DOI=10.1128/aem.57.5.1554-1559.1991;
RA Bahl H., Burchhardt G., Spreinat A., Haeckel K., Wienecke A., Schmidt B.,
RA Antranikian G.;
RT "Alpha-amylase of Clostridium thermosulfurogenes EM1: nucleotide sequence
RT of the gene, processing of the enzyme, and comparison of other alpha-
RT amylases.";
RL Appl. Environ. Microbiol. 57:1554-1559(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 3896 / EM1;
RA Sahm K., Matuschek M., Mueller H., Mitchell W.J., Bahl H.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-255.
RC STRAIN=DSM 3896 / EM1;
RX PubMed=1874408; DOI=10.1016/0378-1097(91)90476-q;
RA Bahl H., Burchhardt G., Wienecke A.;
RT "Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes
RT homologous to Escherichia coli genes encoding integral membrane components
RT of binding protein-dependent transport systems.";
RL FEMS Microbiol. Lett. 65:83-87(1991).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7747949; DOI=10.1128/aem.61.4.1257-1265.1995;
RA Wind R.D., Liebl W., Buitelaar R.M., Penninga D., Spreinat A.,
RA Dijkhuizen L., Bahl H.;
RT "Cyclodextrin formation by the thermostable alpha-amylase of
RT Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the
RT enzyme as a cyclodextrin glycosyltransferase.";
RL Appl. Environ. Microbiol. 61:1257-1265(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 28-710.
RX PubMed=8604143; DOI=10.1006/jmbi.1996.0113;
RA Knegtel R.M.A., Wind R.D., Rozeboom H.J., Kalk K.H., Buitelaar R.M.,
RA Dijkhuizen L., Dijkstra B.W.;
RT "Crystal structure at 2.3 A resolution and revised nucleotide sequence of
RT the thermostable cyclodextrin glycosyltransferase from
RT Thermonanaerobacterium thermosulfurigenes EM1.";
RL J. Mol. Biol. 256:611-622(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 28-710 IN COMPLEX WITH
RP MALTOHEPTAOSE AND CALCIUM IONS.
RC STRAIN=DSM 3896 / EM1;
RX PubMed=9488711; DOI=10.1074/jbc.273.10.5771;
RA Wind R.D., Uitdehaag J.C., Buitelaar R.M., Dijkstra B.W., Dijkhuizen L.;
RT "Engineering of cyclodextrin product specificity and pH optima of the
RT thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium
RT thermosulfurigenes EM1.";
RL J. Biol. Chem. 273:5771-5779(1998).
CC -!- FUNCTION: Degrades starch to alpha-, beta-, and gamma-cyclodextrins, as
CC well as linear sugars.
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;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1854207}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an alpha-amylase.
CC {ECO:0000305|PubMed:1854207}.
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DR EMBL; M57692; AAB00845.1; -; Genomic_DNA.
DR PIR; S63598; S63598.
DR PDB; 1A47; X-ray; 2.56 A; A=28-710.
DR PDB; 1CIU; X-ray; 2.30 A; A=28-710.
DR PDB; 3BMV; X-ray; 1.60 A; A=28-710.
DR PDB; 3BMW; X-ray; 1.60 A; A=28-710.
DR PDBsum; 1A47; -.
DR PDBsum; 1CIU; -.
DR PDBsum; 3BMV; -.
DR PDBsum; 3BMW; -.
DR AlphaFoldDB; P26827; -.
DR SMR; P26827; -.
DR DrugBank; DB03773; alpha-D-quinovopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 2.4.1.19; 1534.
DR SABIO-RK; P26827; -.
DR EvolutionaryTrace; P26827; -.
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; Direct protein sequencing; Glycosyltransferase;
KW Metal-binding; Secreted; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1854207"
FT CHAIN 28..710
FT /note="Cyclomaltodextrin glucanotransferase"
FT /id="PRO_0000001444"
FT DOMAIN 526..603
FT /note="IPT/TIG"
FT DOMAIN 605..710
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:8604143"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:8604143"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 128..129
FT /ligand="substrate"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 221..224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260..261
FT /ligand="substrate"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT BINDING 402
FT /ligand="substrate"
FT SITE 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 128
FT /note="Missing (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..138
FT /note="FKRTNP -> LREQS (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..398
FT /note="EQYMTGNGD -> VYDRQWR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3BMV"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3BMV"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3BMV"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3BMW"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:3BMV"
FT TURN 486..491
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 582..590
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 600..605
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 607..619
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 627..634
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:3BMV"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:3BMV"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 659..667
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 671..682
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:3BMW"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:3BMV"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:3BMV"
SQ SEQUENCE 710 AA; 78417 MW; F5260AE60D3F27D2 CRC64;
MKKTFKLILV LMLSLTLVFG LTAPIQAASD TAVSNVVNYS TDVIYQIVTD RFVDGNTSNN
PTGDLYDPTH TSLKKYFGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YAVLPDSTFG
GSTSYHGYWA RDFKRTNPYF GSFTDFQNLI NTAHAHNIKV IIDFAPNHTS PASETDPTYA
ENGRLYDNGT LLGGYTNDTN GYFHHYGGTD FSSYEDGIYR NLFDLADLNQ QNSTIDSYLK
SAIKVWLDMG IDGIRLDAVK HMPFGWQKNF MDSILSYRPV FTFGEWFLGT NEIDVNNTYF
ANESGMSLLD FRFSQKVRQV FRDNTDTMYG LDSMIQSTAS DYNFINDMVT FIDNHDMDRF
YNGGSTRPVE QALAFTLTSR GVPAIYYGTE QYMTGNGDPY NRAMMTSFNT STTAYNVIKK
LAPLRKSNPA IAYGTTQQRW INNDVYIYER KFGNNVALVA INRNLSTSYN ITGLYTALPA
GTYTDVLGGL LNGNSISVAS DGSVTPFTLS AGEVAVWQYV SSSNSPLIGH VGPTMTKAGQ
TITIDGRGFG TTSGQVLFGS TAGTIVSWDD TEVKVKVPSV TPGKYNISLK TSSGATSNTY
NNINILTGNQ ICVRFVVNNA STVYGENVYL TGNVAELGNW DTSKAIGPMF NQVVYQYPTW
YYDVSVPAGT TIQFKFIKKN GNTITWEGGS NHTYTVPSSS TGTVIVNWQQ
