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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Calcium 1
Metal bindingi57 – 571Calcium 1; via carbonyl oxygen
Metal bindingi60 – 601Calcium 1
Metal bindingi61 – 611Calcium 1
Metal bindingi79 – 791Calcium 1; via carbonyl oxygen
Metal bindingi81 – 811Calcium 1
Metal bindingi166 – 1661Calcium 2
Binding sitei167 – 1671SubstrateBy similarity
Metal bindingi217 – 2171Calcium 2; via carbonyl oxygen
Metal bindingi226 – 2261Calcium 2
Binding sitei254 – 2541SubstrateBy similarity
Active sitei256 – 2561Nucleophile
Metal bindingi260 – 2601Calcium 2; via carbonyl oxygen
Active sitei284 – 2841Proton donor
Binding sitei354 – 3541SubstrateBy similarity
Sitei355 – 3551Transition state stabilizerBy similarity
Binding sitei398 – 3981SubstrateBy similarity
Binding sitei402 – 4021SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.19. 623.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclomaltodextrin glucanotransferase (EC:2.4.1.19)
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name:
CGTase
Gene namesi
Name:cgt
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 711680Cyclomaltodextrin glucanotransferasePRO_0000001442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 78

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 484Combined sources
Helixi50 – 523Combined sources
Helixi58 – 603Combined sources
Helixi64 – 663Combined sources
Helixi69 – 713Combined sources
Helixi82 – 909Combined sources
Turni93 – 986Combined sources
Beta strandi101 – 1044Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi128 – 1358Combined sources
Turni137 – 1393Combined sources
Helixi142 – 15413Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi167 – 1704Combined sources
Turni179 – 1824Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi189 – 1924Combined sources
Helixi213 – 2175Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi224 – 2274Combined sources
Helixi232 – 24615Combined sources
Turni247 – 2493Combined sources
Beta strandi252 – 2565Combined sources
Helixi258 – 2603Combined sources
Helixi264 – 27613Combined sources
Beta strandi280 – 2834Combined sources
Helixi294 – 3029Combined sources
Beta strandi306 – 3083Combined sources
Helixi310 – 32011Combined sources
Helixi327 – 34014Combined sources
Helixi344 – 3463Combined sources
Helixi367 – 37812Combined sources
Beta strandi379 – 3868Combined sources
Helixi389 – 3913Combined sources
Helixi400 – 4023Combined sources
Helixi413 – 42715Combined sources
Helixi429 – 4335Combined sources
Beta strandi435 – 4417Combined sources
Beta strandi443 – 45210Combined sources
Beta strandi455 – 4628Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi480 – 4834Combined sources
Turni486 – 4916Combined sources
Beta strandi496 – 4983Combined sources
Helixi500 – 5023Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi527 – 5326Combined sources
Beta strandi534 – 5363Combined sources
Beta strandi541 – 5477Combined sources
Beta strandi555 – 5584Combined sources
Beta strandi565 – 5673Combined sources
Beta strandi570 – 5767Combined sources
Beta strandi582 – 5909Combined sources
Beta strandi600 – 6056Combined sources
Beta strandi610 – 61910Combined sources
Beta strandi627 – 6348Combined sources
Helixi635 – 6373Combined sources
Helixi642 – 6443Combined sources
Beta strandi652 – 6554Combined sources
Beta strandi660 – 66910Combined sources
Beta strandi671 – 6799Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi693 – 6964Combined sources
Beta strandi699 – 7013Combined sources
Beta strandi703 – 7086Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYGX-ray2.50A32-711[»]
ProteinModelPortaliP31797.
SMRiP31797. Positions 32-711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini526 – 60479IPT/TIGAdd
BLAST
Domaini605 – 711107CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 165134A1Add
BLAST
Regioni127 – 1282Substrate bindingBy similarity
Regioni166 – 22964BAdd
BLAST
Regioni220 – 2234Substrate bindingBy similarity
Regioni230 – 433204A2Add
BLAST
Regioni259 – 2602Substrate bindingBy similarity
Regioni434 – 52289CAdd
BLAST
Regioni523 – 60684DAdd
BLAST
Regioni607 – 711105EAdd
BLAST

Domaini

May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation
Contains 1 IPT/TIG domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRWLSLVLS MSFVFSAIFI VSDTQKVTVE AAGNLNKVNF TSDVVYQIVV
60 70 80 90 100
DRFVDGNTSN NPSGALFSSG CTNLRKYCGG DWQGIINKIN DGYLTDMGVT
110 120 130 140 150
AIWISQPVEN VFSVMNDASG SASYHGYWAR DFKKPNPFFG TLSDFQRLVD
160 170 180 190 200
AAHAKGIKVI IDFAPNHTSP ASETNPSYME NGRLYDNGTL LGGYTNDANM
210 220 230 240 250
YFHHNGGTTF SSLEDGIYRN LFDLADLNHQ NPVIDRYLKD AVKMWIDMGI
260 270 280 290 300
DGIRMDAVKH MPFGWQKSLM DEIDNYRPVF TFGEWFLSEN EVDANNHYFA
310 320 330 340 350
NESGMSLLDF RFGQKLRQVL RNNSDNWYGF NQMIQDTASA YDEVLDQVTF
360 370 380 390 400
IDNHDMDRFM IDGGDPRKVD MALAVLLTSR GVPNIYYGTE QYMTGNGDPN
410 420 430 440 450
NRKMMSSFNK NTRAYQVIQK LSSLRRNNPA LAYGDTEQRW INGDVYVYER
460 470 480 490 500
QFGKDVVLVA VNRSSSSNYS ITGLFTALPA GTYTDQLGGL LDGNTIQVGS
510 520 530 540 550
NGSVNAFDLG PGEVGVWAYS ATESTPIIGH VGPMMGQVGH QVTIDGEGFG
560 570 580 590 600
TNTGTVKFGT TAANVVSWSN NQIVVAVPNV SPGKYNITVQ SSSGQTSAAY
610 620 630 640 650
DNFEVLTNDQ VSVRFVVNNA TTNLGQNIYI VGNVYELGNW DTSKAIGPMF
660 670 680 690 700
NQVVYSYPTW YIDVSVPEGK TIEFKFIKKD SQGNVTWESG SNHVYTTPTN
710
TTGKIIVDWQ N
Length:711
Mass (Da):78,923
Last modified:July 1, 1993 - v1
Checksum:i5F9F71FF01C2CC60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti460 – 4601A → R AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59042 Genomic DNA. Translation: CAA41770.1.
X59043 Genomic DNA. Translation: CAA41771.1.
X59044 Genomic DNA. Translation: CAA41772.1.
PIRiS26588. ALBSXF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59042 Genomic DNA. Translation: CAA41770.1.
X59043 Genomic DNA. Translation: CAA41771.1.
X59044 Genomic DNA. Translation: CAA41772.1.
PIRiS26588. ALBSXF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYGX-ray2.50A32-711[»]
ProteinModelPortaliP31797.
SMRiP31797. Positions 32-711.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.4.1.19. 623.

Miscellaneous databases

EvolutionaryTraceiP31797.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme."
    Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K., Imanaka T.
    Appl. Environ. Microbiol. 58:4016-4025(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NO. 2.
  2. "Polypeptide possessing cyclomaltodextrin glucanotransferase activity."
    Sugimoto T., Kubota M., Sakai S.
    Patent number GB2169902, 23-JUL-1986
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-41.
  3. Kubota M., Matsuura Y., Sakai S., Katsube Y.
    Submitted (FEB-1993) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS.

Entry informationi

Entry nameiCDGT_GEOSE
AccessioniPrimary (citable) accession number: P31797
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.