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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus sp. (strain 1011)
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 bindingi54 – 541Calcium 1
Metal bindingi56 – 561Calcium 1; via carbonyl oxygen
Metal bindingi59 – 591Calcium 1
Metal bindingi60 – 601Calcium 1
Metal bindingi78 – 781Calcium 1; via carbonyl oxygen
Metal bindingi80 – 801Calcium 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 – 3981Substrate
Binding sitei402 – 4021Substrate

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. 691.

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
OrganismiBacillus sp. (strain 1011)
Taxonomic identifieri1410 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 713686Cyclomaltodextrin glucanotransferasePRO_0000001437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 77

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 463Combined sources
Helixi49 – 513Combined sources
Helixi57 – 593Combined sources
Helixi63 – 653Combined sources
Helixi81 – 899Combined sources
Turni90 – 934Combined sources
Helixi94 – 963Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1213Combined 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
Beta strandi194 – 1963Combined sources
Beta strandi210 – 2123Combined sources
Helixi213 – 2186Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi224 – 2274Combined sources
Helixi232 – 24716Combined sources
Beta strandi252 – 2554Combined sources
Helixi258 – 2603Combined sources
Helixi263 – 27614Combined sources
Beta strandi280 – 2834Combined sources
Helixi294 – 3029Combined sources
Beta strandi303 – 3086Combined sources
Helixi310 – 32011Combined sources
Helixi327 – 34014Combined sources
Beta strandi341 – 3433Combined sources
Helixi344 – 3463Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi362 – 3643Combined sources
Helixi366 – 37813Combined sources
Beta strandi379 – 3868Combined sources
Helixi389 – 3913Combined sources
Helixi400 – 4023Combined sources
Helixi413 – 4219Combined sources
Helixi424 – 4274Combined sources
Helixi429 – 4335Combined sources
Beta strandi435 – 4417Combined sources
Beta strandi443 – 45210Combined sources
Beta strandi455 – 4628Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi473 – 4753Combined 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 strandi561 – 5633Combined sources
Helixi565 – 5673Combined sources
Beta strandi568 – 5714Combined sources
Beta strandi573 – 5797Combined sources
Beta strandi585 – 5939Combined sources
Beta strandi603 – 6086Combined sources
Beta strandi610 – 62213Combined sources
Beta strandi630 – 6378Combined sources
Helixi638 – 6403Combined sources
Turni641 – 6433Combined sources
Helixi645 – 6473Combined sources
Beta strandi655 – 6584Combined sources
Beta strandi663 – 6708Combined sources
Beta strandi673 – 68311Combined sources
Beta strandi686 – 6894Combined sources
Beta strandi695 – 6984Combined sources
Beta strandi701 – 71010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7FX-ray1.90A/B28-713[»]
1DEDX-ray2.00A/B28-713[»]
1I75X-ray2.00A/B28-713[»]
1PAMX-ray1.80A/B28-713[»]
1UKQX-ray2.00A/B28-713[»]
1UKSX-ray1.90A/B28-713[»]
1UKTX-ray2.20A/B28-713[»]
1V3JX-ray2.00A/B28-713[»]
1V3KX-ray2.00A/B28-713[»]
1V3LX-ray2.10A/B28-713[»]
1V3MX-ray2.00A/B28-713[»]
ProteinModelPortaliP05618.
SMRiP05618. Positions 28-713.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05618.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini526 – 60782IPT/TIGAdd
BLAST
Domaini608 – 713106CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 165138A1Add
BLAST
Regioni127 – 1282Substrate binding
Regioni166 – 22964BAdd
BLAST
Regioni220 – 2234Substrate binding
Regioni230 – 433204A2Add
BLAST
Regioni259 – 2602Substrate bindingBy similarity
Regioni434 – 52289CAdd
BLAST
Regioni523 – 60987DAdd
BLAST
Regioni610 – 713104EAdd
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.

P05618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD
60 70 80 90 100
RFSDGNPANN PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA
110 120 130 140 150
IWISQPVENI YSVINYSGVN NTAYHGYWAR DFKKTNPAYG TMQDFKNLID
160 170 180 190 200
TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE NGRLYDNGNL LGGYTNDTQN
210 220 230 240 250
LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD AIKMWLDLGV
260 270 280 290 300
DGIRVDAVKH MPFGWQKSFM ATINNYKPVF TFGEWFLGVN EISPEYHQFA
310 320 330 340 350
NESGMSLLDF RFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF
360 370 380 390 400
IDNHDMERFH TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD
410 420 430 440 450
NRARLPSFST TTTAYQVIQK LAPLRKSNPA IAYGSTHERW INNDVIIYER
460 470 480 490 500
KFGNNVAVVA INRNMNTPAS ITGLVTSLRR ASYNDVLGGI LNGNTLTVGA
510 520 530 540 550
GGAASNFTLA PGGTAVWQYT TDATTPIIGN VGPMMAKPGV TITIDGRGFG
560 570 580 590 600
SGKGTVYFGT TAVTGADIVA WEDTQIQVKI PAVPGGIYDI RVANAAGAAS
610 620 630 640 650
NIYDNFEVLT GDQVTVRFVI NNATTALGQN VFLTGNVSEL GNWDPNNAIG
660 670 680 690 700
PMYNQVVYQY PTWYYDVSVP AGQTIEFKFL KKQGSTVTWE GGANRTFTTP
710
TSGTATVNVN WQP
Length:713
Mass (Da):78,340
Last modified:November 1, 1988 - v1
Checksum:i524B259526B56C52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17366 Genomic DNA. Translation: AAA22308.1.
PIRiA26678. ALBSG1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17366 Genomic DNA. Translation: AAA22308.1.
PIRiA26678. ALBSG1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7FX-ray1.90A/B28-713[»]
1DEDX-ray2.00A/B28-713[»]
1I75X-ray2.00A/B28-713[»]
1PAMX-ray1.80A/B28-713[»]
1UKQX-ray2.00A/B28-713[»]
1UKSX-ray1.90A/B28-713[»]
1UKTX-ray2.20A/B28-713[»]
1V3JX-ray2.00A/B28-713[»]
1V3KX-ray2.00A/B28-713[»]
1V3LX-ray2.10A/B28-713[»]
1V3MX-ray2.00A/B28-713[»]
ProteinModelPortaliP05618.
SMRiP05618. Positions 28-713.
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. 691.

Miscellaneous databases

EvolutionaryTraceiP05618.

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. "Nucleotide sequence of the beta-cyclodextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of alpha-amylases."
    Kimura K., Kataoka S., Ishii Y., Takano T., Yamane K.
    J. Bacteriol. 169:4399-4402(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus Sp. 1011. Comparison of two independent molecules at 1.8-A resolution."
    Harata K., Haga K., Nakamura A., Aoyagi M., Yamane K.
    Acta Crystallogr. D 52:1136-1145(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-713.

Entry informationi

Entry nameiCDGT_BACS0
AccessioniPrimary (citable) accession number: P05618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 11, 2016
This is version 119 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

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.