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Protein

Cyclomaltodextrin glucanotransferase

Gene
N/A
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.

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi61Calcium 11
Metal bindingi63Calcium 1; via carbonyl oxygen1
Metal bindingi66Calcium 11
Metal bindingi67Calcium 11
Metal bindingi85Calcium 1; via carbonyl oxygen1
Metal bindingi87Calcium 11
Metal bindingi173Calcium 21
Binding sitei174Substrate1
Metal bindingi224Calcium 2; via carbonyl oxygen1
Binding sitei230Substrate1
Metal bindingi233Calcium 21
Binding sitei261SubstrateBy similarity1
Active sitei263NucleophileBy similarity1
Metal bindingi267Calcium 2; via carbonyl oxygen1
Binding sitei267Substrate1
Active sitei291Proton donorBy similarity1
Binding sitei361Substrate1
Sitei362Transition state stabilizerBy similarity1
Binding sitei405Substrate1
Binding sitei409Substrate1

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.

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
OrganismiBacillus circulans
Taxonomic identifieri1397 [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 – 34Add BLAST34
ChainiPRO_000000143035 – 718Cyclomaltodextrin glucanotransferaseAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi77 ↔ 84

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1718
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 39Combined sources3
Beta strandi51 – 53Combined sources3
Helixi56 – 59Combined sources4
Helixi64 – 66Combined sources3
Helixi70 – 72Combined sources3
Helixi88 – 96Combined sources9
Helixi99 – 103Combined sources5
Beta strandi107 – 110Combined sources4
Beta strandi114 – 116Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi135 – 142Combined sources8
Turni144 – 146Combined sources3
Helixi149 – 161Combined sources13
Beta strandi165 – 170Combined sources6
Beta strandi174 – 177Combined sources4
Turni186 – 189Combined sources4
Beta strandi191 – 193Combined sources3
Beta strandi196 – 199Combined sources4
Beta strandi201 – 203Combined sources3
Beta strandi217 – 219Combined sources3
Helixi220 – 225Combined sources6
Beta strandi226 – 228Combined sources3
Beta strandi231 – 234Combined sources4
Helixi239 – 254Combined sources16
Beta strandi259 – 263Combined sources5
Helixi265 – 267Combined sources3
Helixi270 – 283Combined sources14
Beta strandi287 – 290Combined sources4
Beta strandi295 – 298Combined sources4
Helixi301 – 309Combined sources9
Beta strandi310 – 315Combined sources6
Helixi317 – 327Combined sources11
Helixi334 – 347Combined sources14
Helixi351 – 353Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi369 – 371Combined sources3
Helixi373 – 385Combined sources13
Beta strandi386 – 393Combined sources8
Helixi396 – 398Combined sources3
Helixi407 – 409Combined sources3
Helixi420 – 428Combined sources9
Helixi431 – 434Combined sources4
Helixi436 – 440Combined sources5
Beta strandi442 – 448Combined sources7
Beta strandi450 – 459Combined sources10
Beta strandi462 – 469Combined sources8
Beta strandi476 – 478Combined sources3
Beta strandi487 – 490Combined sources4
Turni493 – 498Combined sources6
Beta strandi503 – 506Combined sources4
Beta strandi513 – 515Combined sources3
Beta strandi520 – 525Combined sources6
Beta strandi533 – 538Combined sources6
Beta strandi540 – 542Combined sources3
Beta strandi547 – 553Combined sources7
Beta strandi561 – 564Combined sources4
Beta strandi567 – 569Combined sources3
Helixi571 – 573Combined sources3
Beta strandi574 – 577Combined sources4
Beta strandi579 – 585Combined sources7
Beta strandi591 – 600Combined sources10
Beta strandi608 – 613Combined sources6
Beta strandi615 – 626Combined sources12
Beta strandi635 – 642Combined sources8
Helixi643 – 645Combined sources3
Turni646 – 648Combined sources3
Beta strandi651 – 655Combined sources5
Beta strandi661 – 664Combined sources4
Beta strandi669 – 676Combined sources8
Beta strandi680 – 691Combined sources12
Beta strandi693 – 695Combined sources3
Beta strandi701 – 704Combined sources4
Beta strandi707 – 716Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CGTX-ray2.00A35-718[»]
1CGUX-ray2.50A35-718[»]
3CGTX-ray2.40A35-718[»]
4CGTX-ray2.60A35-718[»]
5CGTX-ray2.50A35-718[»]
6CGTX-ray2.60A35-718[»]
7CGTX-ray3.00A35-718[»]
8CGTX-ray2.40A35-718[»]
9CGTX-ray2.50A35-718[»]
ProteinModelPortaliP30920.
SMRiP30920.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30920.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini532 – 612IPT/TIGAdd BLAST81
Domaini613 – 718CBM20PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 172A1Add BLAST138
Regioni134 – 135Substrate binding2
Regioni173 – 236BAdd BLAST64
Regioni227 – 230Substrate bindingBy similarity4
Regioni237 – 440A2Add BLAST204
Regioni266 – 267Substrate binding2
Regioni441 – 528CAdd BLAST88
Regioni529 – 614DAdd BLAST86
Regioni615 – 718EAdd 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.
IPR006311. TAT_signal.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 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.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV
60 70 80 90 100
IYQVFTDRFL DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF
110 120 130 140 150
SDLGVTALWI SQPVENIFAT INYSGVTNTA YHGYWARDFK KTNPYFGTMA
160 170 180 190 200
DFQNLITTAH AKGIKIVIDF APNHTSPAME TDTSFAENGR LYDNGTLVGG
210 220 230 240 250
YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT IDKYFKDAIK
260 270 280 290 300
LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD
310 320 330 340 350
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ
360 370 380 390 400
VNDQVTFIDN HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL
410 420 430 440 450
TGNGDPDNRA KMPSFSKSTT AFNVISKLAP LRKSNPAIAY GSTQQRWINN
460 470 480 490 500
DVYVYERKFG KSVAVVAVNR NLSTSASITG LSTSLPTGSY TDVLGGVLNG
510 520 530 540 550
NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV MGKPGNVVTI
560 570 580 590 600
DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA
610 620 630 640 650
SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST
660 670 680 690 700
GSTAIGPAFN QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN
710
HTFTTPASGT ATVTVNWQ
Length:718
Mass (Da):78,047
Last modified:July 1, 1993 - v1
Checksum:iE08CF0FE9C98BDA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68326 Genomic DNA. Translation: CAA48401.1.
PIRiS23674. ALBSGC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68326 Genomic DNA. Translation: CAA48401.1.
PIRiS23674. ALBSGC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CGTX-ray2.00A35-718[»]
1CGUX-ray2.50A35-718[»]
3CGTX-ray2.40A35-718[»]
4CGTX-ray2.60A35-718[»]
5CGTX-ray2.50A35-718[»]
6CGTX-ray2.60A35-718[»]
7CGTX-ray3.00A35-718[»]
8CGTX-ray2.40A35-718[»]
9CGTX-ray2.50A35-718[»]
ProteinModelPortaliP30920.
SMRiP30920.
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.

Miscellaneous databases

EvolutionaryTraceiP30920.

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.
IPR006311. TAT_signal.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 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.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDGT1_BACCI
AccessioniPrimary (citable) accession number: P30920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 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.