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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus circulans
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.1 Publication

Cofactori

Ca2+Note: Binds 3 Ca2+ 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 sitei167Substrate1
Metal bindingi217Calcium 2; via carbonyl oxygen1
Metal bindingi226Calcium 21
Binding sitei254Substrate1
Active sitei256Nucleophile1
Metal bindingi260Calcium 2; via carbonyl oxygen1
Active sitei284Proton donor1
Metal bindingi342Calcium 3; via carbonyl oxygen1
Binding sitei354Substrate1
Sitei355Transition state stabilizerBy similarity1
Binding sitei398Substrate1
Binding sitei402Substrate1
Metal bindingi604Calcium 31

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. 649.
SABIO-RKP43379.

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 circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi256D → N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355. 1 Publication1
Mutagenesisi284E → Q: Reduces activity 4100-fold. 1 Publication1
Mutagenesisi355D → N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000000143128 – 713Cyclomaltodextrin glucanotransferaseAdd BLAST686

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi70 ↔ 771 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 47Combined sources4
Helixi49 – 51Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 65Combined sources3
Helixi81 – 89Combined sources9
Turni90 – 97Combined sources8
Beta strandi100 – 103Combined sources4
Beta strandi107 – 109Combined sources3
Beta strandi114 – 118Combined sources5
Beta strandi119 – 121Combined sources3
Helixi123 – 125Combined 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 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 – 274Combined sources12
Beta strandi280 – 283Combined sources4
Helixi294 – 302Combined sources9
Beta strandi303 – 308Combined sources6
Helixi310 – 320Combined sources11
Helixi327 – 340Combined sources14
Helixi344 – 346Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi362 – 364Combined sources3
Helixi366 – 377Combined sources12
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 – 451Combined sources9
Beta strandi453 – 462Combined sources10
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 – 520Combined sources7
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 – 621Combined sources12
Beta strandi630 – 637Combined sources8
Helixi638 – 640Combined sources3
Turni641 – 643Combined sources3
Helixi645 – 647Combined sources3
Beta strandi655 – 658Combined sources4
Beta strandi663 – 670Combined sources8
Beta strandi674 – 683Combined sources10
Beta strandi686 – 689Combined sources4
Beta strandi691 – 693Combined sources3
Beta strandi695 – 698Combined sources4
Beta strandi701 – 703Combined sources3
Beta strandi705 – 710Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDGX-ray2.00A28-713[»]
1CGVX-ray2.50A28-713[»]
1CGWX-ray2.50A28-713[»]
1CGXX-ray2.50A28-713[»]
1CGYX-ray2.50A28-713[»]
1CXEX-ray2.10A28-713[»]
1CXFX-ray2.10A28-713[»]
1CXHX-ray2.41A28-713[»]
1CXIX-ray2.20A28-713[»]
1CXKX-ray2.09A28-713[»]
1CXLX-ray1.81A28-713[»]
1D3CX-ray1.78A28-713[»]
1DTUX-ray2.40A28-713[»]
1EO5X-ray2.00A28-713[»]
1EO7X-ray2.48A28-713[»]
1KCKX-ray2.43A28-713[»]
1KCLX-ray1.94A28-713[»]
1OT1X-ray2.00A28-713[»]
1OT2X-ray2.10A28-713[»]
1PEZX-ray2.32A28-713[»]
1PJ9X-ray2.00A28-713[»]
1TCMX-ray2.20A/B28-713[»]
2CXGX-ray2.50A28-713[»]
2DIJX-ray2.60A28-713[»]
ProteinModelPortaliP43379.
SMRiP43379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43379.

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
Regioni172 – 174Substrate binding3
Regioni220 – 223Substrate binding4
Regioni230 – 433A2Add BLAST204
Regioni259 – 260Substrate binding2
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.

P43379-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFLKSTAA LALGLSLTFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD
60 70 80 90 100
RFSDGNPANN PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA
110 120 130 140 150
IWISQPVENI YSIINYSGVN NTAYHGYWAR DFKKTNPAYG TIADFQNLIA
160 170 180 190 200
AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE NGRLYDNGTL LGGYTNDTQN
210 220 230 240 250
LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDVYLKD AIKMWLDLGI
260 270 280 290 300
DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVSPENHKFA
310 320 330 340 350
NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF
360 370 380 390 400
IDNHDMERFH ASNANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGTDPD
410 420 430 440 450
NRARIPSFST STTAYQVIQK LAPLRKCNPA IAYGSTQERW INNDVLIYER
460 470 480 490 500
KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ GSYNDVLGGL LNGNTLSVGS
510 520 530 540 550
GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV TITIDGRGFG
560 570 580 590 600
SSKGTVYFGT TAVSGADITS WEDTQIKVKI PAVAGGNYNI KVANAAGTAS
610 620 630 640 650
NVYDNFEVLS GDQVSVRFVV NNATTALGQN VYLTGSVSEL GNWDPAKAIG
660 670 680 690 700
PMYNQVVYQY PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP
710
SSGTATINVN WQP
Length:713
Mass (Da):77,309
Last modified:November 1, 1995 - v1
Checksum:i8ABBFB2C633A004B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78145 Genomic DNA. Translation: CAA55023.1.
PIRiA58800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78145 Genomic DNA. Translation: CAA55023.1.
PIRiA58800.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDGX-ray2.00A28-713[»]
1CGVX-ray2.50A28-713[»]
1CGWX-ray2.50A28-713[»]
1CGXX-ray2.50A28-713[»]
1CGYX-ray2.50A28-713[»]
1CXEX-ray2.10A28-713[»]
1CXFX-ray2.10A28-713[»]
1CXHX-ray2.41A28-713[»]
1CXIX-ray2.20A28-713[»]
1CXKX-ray2.09A28-713[»]
1CXLX-ray1.81A28-713[»]
1D3CX-ray1.78A28-713[»]
1DTUX-ray2.40A28-713[»]
1EO5X-ray2.00A28-713[»]
1EO7X-ray2.48A28-713[»]
1KCKX-ray2.43A28-713[»]
1KCLX-ray1.94A28-713[»]
1OT1X-ray2.00A28-713[»]
1OT2X-ray2.10A28-713[»]
1PEZX-ray2.32A28-713[»]
1PJ9X-ray2.00A28-713[»]
1TCMX-ray2.20A/B28-713[»]
2CXGX-ray2.50A28-713[»]
2DIJX-ray2.60A28-713[»]
ProteinModelPortaliP43379.
SMRiP43379.
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. 649.
SABIO-RKP43379.

Miscellaneous databases

EvolutionaryTraceiP43379.

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 nameiCDGT2_BACCI
AccessioniPrimary (citable) accession number: P43379
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 115 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.