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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)DescriptionActionsGraphical viewLength
Metal bindingi54Calcium 11
Metal bindingi56Calcium 1; via carbonyl oxygen1
Metal bindingi59Calcium 11
Metal bindingi60Calcium 11
Metal bindingi78Calcium 1; via carbonyl oxygen1
Metal bindingi80Calcium 11
Metal bindingi166Calcium 21
Binding sitei167SubstrateBy similarity1
Metal bindingi217Calcium 2; via carbonyl oxygen1
Metal bindingi226Calcium 21
Binding sitei254SubstrateBy similarity1
Active sitei256Nucleophile1
Metal bindingi260Calcium 2; via carbonyl oxygen1
Active sitei284Proton donor1
Binding sitei354SubstrateBy similarity1
Sitei355Transition state stabilizerBy similarity1
Binding sitei398Substrate1
Binding sitei402Substrate1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000000143728 – 713Cyclomaltodextrin glucanotransferaseAdd BLAST686

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi70 ↔ 77

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 46Combined sources3
Helixi49 – 51Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 65Combined sources3
Helixi81 – 89Combined sources9
Turni90 – 93Combined sources4
Helixi94 – 96Combined sources3
Beta strandi100 – 103Combined sources4
Beta strandi107 – 109Combined sources3
Beta strandi114 – 116Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi128 – 135Combined sources8
Turni137 – 139Combined sources3
Helixi142 – 154Combined sources13
Beta strandi158 – 163Combined sources6
Beta strandi167 – 170Combined sources4
Turni179 – 182Combined sources4
Beta strandi184 – 186Combined sources3
Beta strandi189 – 192Combined sources4
Beta strandi194 – 196Combined sources3
Beta strandi210 – 212Combined sources3
Helixi213 – 218Combined sources6
Beta strandi219 – 221Combined sources3
Beta strandi224 – 227Combined sources4
Helixi232 – 247Combined sources16
Beta strandi252 – 255Combined sources4
Helixi258 – 260Combined sources3
Helixi263 – 276Combined sources14
Beta strandi280 – 283Combined sources4
Helixi294 – 302Combined sources9
Beta strandi303 – 308Combined sources6
Helixi310 – 320Combined sources11
Helixi327 – 340Combined sources14
Beta strandi341 – 343Combined sources3
Helixi344 – 346Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi362 – 364Combined sources3
Helixi366 – 378Combined sources13
Beta strandi379 – 386Combined sources8
Helixi389 – 391Combined sources3
Helixi400 – 402Combined sources3
Helixi413 – 421Combined sources9
Helixi424 – 427Combined sources4
Helixi429 – 433Combined sources5
Beta strandi435 – 441Combined sources7
Beta strandi443 – 452Combined sources10
Beta strandi455 – 462Combined sources8
Beta strandi465 – 467Combined sources3
Beta strandi469 – 471Combined sources3
Beta strandi473 – 475Combined sources3
Beta strandi480 – 483Combined sources4
Turni486 – 491Combined sources6
Beta strandi496 – 498Combined sources3
Helixi500 – 502Combined sources3
Beta strandi507 – 509Combined sources3
Beta strandi514 – 519Combined sources6
Beta strandi527 – 532Combined sources6
Beta strandi534 – 536Combined sources3
Beta strandi541 – 547Combined sources7
Beta strandi555 – 558Combined sources4
Beta strandi561 – 563Combined sources3
Helixi565 – 567Combined sources3
Beta strandi568 – 571Combined sources4
Beta strandi573 – 579Combined sources7
Beta strandi585 – 593Combined sources9
Beta strandi603 – 608Combined sources6
Beta strandi610 – 622Combined sources13
Beta strandi630 – 637Combined sources8
Helixi638 – 640Combined sources3
Turni641 – 643Combined sources3
Helixi645 – 647Combined sources3
Beta strandi655 – 658Combined sources4
Beta strandi663 – 670Combined sources8
Beta strandi673 – 683Combined sources11
Beta strandi686 – 689Combined sources4
Beta strandi695 – 698Combined sources4
Beta strandi701 – 710Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05618.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini526 – 607IPT/TIGAdd BLAST82
Domaini608 – 713CBM20PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 165A1Add BLAST138
Regioni127 – 128Substrate binding2
Regioni166 – 229BAdd BLAST64
Regioni220 – 223Substrate binding4
Regioni230 – 433A2Add BLAST204
Regioni259 – 260Substrate bindingBy similarity2
Regioni434 – 522CAdd BLAST89
Regioni523 – 609DAdd BLAST87
Regioni610 – 713EAdd BLAST104

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
PDB 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.
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...

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: November 2, 2016
This is version 121 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.