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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Calcium 1
Metal bindingi63 – 631Calcium 1; via carbonyl oxygen
Metal bindingi66 – 661Calcium 1
Metal bindingi67 – 671Calcium 1
Metal bindingi85 – 851Calcium 1; via carbonyl oxygen
Metal bindingi87 – 871Calcium 1
Metal bindingi173 – 1731Calcium 2
Binding sitei174 – 1741Substrate
Metal bindingi224 – 2241Calcium 2; via carbonyl oxygen
Binding sitei230 – 2301Substrate
Metal bindingi233 – 2331Calcium 2
Binding sitei261 – 2611SubstrateBy similarity
Active sitei263 – 2631NucleophileBy similarity
Metal bindingi267 – 2671Calcium 2; via carbonyl oxygen
Binding sitei267 – 2671Substrate
Active sitei291 – 2911Proton donorBy similarity
Binding sitei361 – 3611Substrate
Sitei362 – 3621Transition state stabilizerBy similarity
Binding sitei405 – 4051Substrate
Binding sitei409 – 4091Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Add
BLAST
Chaini35 – 718684Cyclomaltodextrin glucanotransferasePRO_0000001430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 84

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
718
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393Combined sources
Beta strandi51 – 533Combined sources
Helixi56 – 594Combined sources
Helixi64 – 663Combined sources
Helixi70 – 723Combined sources
Helixi88 – 969Combined sources
Helixi99 – 1035Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi135 – 1428Combined sources
Turni144 – 1463Combined sources
Helixi149 – 16113Combined sources
Beta strandi165 – 1706Combined sources
Beta strandi174 – 1774Combined sources
Turni186 – 1894Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi196 – 1994Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi217 – 2193Combined sources
Helixi220 – 2256Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 2344Combined sources
Helixi239 – 25416Combined sources
Beta strandi259 – 2635Combined sources
Helixi265 – 2673Combined sources
Helixi270 – 28314Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi295 – 2984Combined sources
Helixi301 – 3099Combined sources
Beta strandi310 – 3156Combined sources
Helixi317 – 32711Combined sources
Helixi334 – 34714Combined sources
Helixi351 – 3533Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi369 – 3713Combined sources
Helixi373 – 38513Combined sources
Beta strandi386 – 3938Combined sources
Helixi396 – 3983Combined sources
Helixi407 – 4093Combined sources
Helixi420 – 4289Combined sources
Helixi431 – 4344Combined sources
Helixi436 – 4405Combined sources
Beta strandi442 – 4487Combined sources
Beta strandi450 – 45910Combined sources
Beta strandi462 – 4698Combined sources
Beta strandi476 – 4783Combined sources
Beta strandi487 – 4904Combined sources
Turni493 – 4986Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi520 – 5256Combined sources
Beta strandi533 – 5386Combined sources
Beta strandi540 – 5423Combined sources
Beta strandi547 – 5537Combined sources
Beta strandi561 – 5644Combined sources
Beta strandi567 – 5693Combined sources
Helixi571 – 5733Combined sources
Beta strandi574 – 5774Combined sources
Beta strandi579 – 5857Combined sources
Beta strandi591 – 60010Combined sources
Beta strandi608 – 6136Combined sources
Beta strandi615 – 62612Combined sources
Beta strandi635 – 6428Combined sources
Helixi643 – 6453Combined sources
Turni646 – 6483Combined sources
Beta strandi651 – 6555Combined sources
Beta strandi661 – 6644Combined sources
Beta strandi669 – 6768Combined sources
Beta strandi680 – 69112Combined sources
Beta strandi693 – 6953Combined sources
Beta strandi701 – 7044Combined sources
Beta strandi707 – 71610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 35-718.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30920.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 61281IPT/TIGAdd
BLAST
Domaini613 – 718106CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 172138A1Add
BLAST
Regioni134 – 1352Substrate binding
Regioni173 – 23664BAdd
BLAST
Regioni227 – 2304Substrate bindingBy similarity
Regioni237 – 440204A2Add
BLAST
Regioni266 – 2672Substrate binding
Regioni441 – 52888CAdd
BLAST
Regioni529 – 61486DAdd
BLAST
Regioni615 – 718104EAdd
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.
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
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. Positions 35-718.
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: 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

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.