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P43379

- CDGT2_BACCI

UniProt

P43379 - CDGT2_BACCI

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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus circulans
Status
Reviewed - 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

Binds 3 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 – 1671Substrate
Metal bindingi217 – 2171Calcium 2; via carbonyl oxygen
Metal bindingi226 – 2261Calcium 2
Binding sitei254 – 2541Substrate
Active sitei256 – 2561Nucleophile
Metal bindingi260 – 2601Calcium 2; via carbonyl oxygen
Active sitei284 – 2841Proton donor
Metal bindingi342 – 3421Calcium 3; via carbonyl oxygen
Binding sitei354 – 3541Substrate
Sitei355 – 3551Transition state stabilizerBy similarity
Binding sitei398 – 3981Substrate
Binding sitei402 – 4021Substrate
Metal bindingi604 – 6041Calcium 3

GO - Molecular functioni

  1. cyclomaltodextrin glucanotransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. starch binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561D → N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355. 1 Publication
Mutagenesisi284 – 2841E → Q: Reduces activity 4100-fold. 1 Publication
Mutagenesisi355 – 3551D → N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 713686Cyclomaltodextrin glucanotransferasePRO_0000001431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 771 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 474
Helixi49 – 513
Helixi57 – 593
Helixi63 – 653
Helixi81 – 899
Turni90 – 978
Beta strandi100 – 1034
Beta strandi107 – 1093
Beta strandi114 – 1185
Beta strandi119 – 1213
Helixi123 – 1253
Beta strandi128 – 1358
Turni137 – 1393
Helixi142 – 15413
Beta strandi158 – 1636
Beta strandi167 – 1704
Turni179 – 1824
Beta strandi184 – 1863
Beta strandi189 – 1924
Beta strandi210 – 2123
Helixi213 – 2186
Beta strandi219 – 2213
Beta strandi224 – 2274
Helixi232 – 24716
Beta strandi252 – 2554
Helixi258 – 2603
Helixi263 – 27412
Beta strandi280 – 2834
Helixi294 – 3029
Beta strandi303 – 3086
Helixi310 – 32011
Helixi327 – 34014
Helixi344 – 3463
Beta strandi347 – 3493
Beta strandi354 – 3563
Beta strandi362 – 3643
Helixi366 – 37712
Beta strandi379 – 3868
Helixi389 – 3913
Helixi400 – 4023
Helixi413 – 4219
Helixi424 – 4274
Helixi429 – 4335
Beta strandi435 – 4417
Beta strandi443 – 4519
Beta strandi453 – 46210
Beta strandi469 – 4713
Beta strandi473 – 4753
Beta strandi480 – 4834
Turni486 – 4916
Beta strandi496 – 4983
Helixi500 – 5023
Beta strandi507 – 5093
Beta strandi514 – 5207
Beta strandi527 – 5326
Beta strandi534 – 5363
Beta strandi541 – 5477
Beta strandi555 – 5584
Beta strandi561 – 5633
Helixi565 – 5673
Beta strandi568 – 5714
Beta strandi573 – 5797
Beta strandi585 – 5939
Beta strandi603 – 6086
Beta strandi610 – 62112
Beta strandi630 – 6378
Helixi638 – 6403
Turni641 – 6433
Helixi645 – 6473
Beta strandi655 – 6584
Beta strandi663 – 6708
Beta strandi674 – 68310
Beta strandi686 – 6894
Beta strandi691 – 6933
Beta strandi695 – 6984
Beta strandi701 – 7033
Beta strandi705 – 7106

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 28-713.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43379.

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
Regioni172 – 1743Substrate binding
Regioni220 – 2234Substrate binding
Regioni230 – 433204A2Add
BLAST
Regioni259 – 2602Substrate binding
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_b_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
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:
EMBL
GenBank
DDBJ
Links Updated
X78145 Genomic DNA. Translation: CAA55023.1.
PIRiA58800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78145 Genomic DNA. Translation: CAA55023.1 .
PIRi A58800.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CDG X-ray 2.00 A 28-713 [» ]
1CGV X-ray 2.50 A 28-713 [» ]
1CGW X-ray 2.50 A 28-713 [» ]
1CGX X-ray 2.50 A 28-713 [» ]
1CGY X-ray 2.50 A 28-713 [» ]
1CXE X-ray 2.10 A 28-713 [» ]
1CXF X-ray 2.10 A 28-713 [» ]
1CXH X-ray 2.41 A 28-713 [» ]
1CXI X-ray 2.20 A 28-713 [» ]
1CXK X-ray 2.09 A 28-713 [» ]
1CXL X-ray 1.81 A 28-713 [» ]
1D3C X-ray 1.78 A 28-713 [» ]
1DTU X-ray 2.40 A 28-713 [» ]
1EO5 X-ray 2.00 A 28-713 [» ]
1EO7 X-ray 2.48 A 28-713 [» ]
1KCK X-ray 2.43 A 28-713 [» ]
1KCL X-ray 1.94 A 28-713 [» ]
1OT1 X-ray 2.00 A 28-713 [» ]
1OT2 X-ray 2.10 A 28-713 [» ]
1PEZ X-ray 2.32 A 28-713 [» ]
1PJ9 X-ray 2.00 A 28-713 [» ]
1TCM X-ray 2.20 A/B 28-713 [» ]
2CXG X-ray 2.50 A 28-713 [» ]
2DIJ X-ray 2.60 A 28-713 [» ]
ProteinModelPortali P43379.
SMRi P43379. Positions 28-713.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.4.1.19. 649.
SABIO-RK P43379.

Miscellaneous databases

EvolutionaryTracei P43379.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS51166. CBM20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form."
    Lawson C.L., van Montfort R., Strokopytov B., Rozeboom H.J., Kalk K.H., de Vries G.E., Penninga D., Dijkhuizen L., Dijkstra B.W.
    J. Mol. Biol. 236:590-600(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Strain: 251.
  2. "X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases."
    Strokopytov B., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
    Biochemistry 34:2234-2240(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-713 IN COMPLEX WITH ACARBOSE.
  3. "Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products."
    Knegtel R.M.A., Strokopytov B., Penninga D., Faber O.G., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
    J. Biol. Chem. 270:29256-29264(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-256/GLN-284, ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-256; GLU-284 AND ASP-355.
    Strain: 251.
  4. "The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251."
    Penninga D., van der Veen B.A., Knegtel R.M.A., van Hijum S.A.F.T., Rozeboom H.J., Kalk K.H., Dijkstra B.W., Dijkhuizen L.
    J. Biol. Chem. 271:32777-32784(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  5. "Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6-A resolution. Implications for product specificity."
    Strokopytov B., Knegtel R.M.A., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
    Biochemistry 35:4241-4249(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
    Strain: 251.
  6. "X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family."
    Uitdehaag J.C., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., Withers S.G., Dijkstra B.W.
    Nat. Struct. Biol. 6:432-436(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 28-713 OF MUTANT ASN-256/GLN-284 IN COMPLEXES WITH CALCIUM IONS AND MALTOTETRAOSE, ACTIVE SITE, DISULFIDE BOND.

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: October 29, 2014
This is version 107 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

External Data

Dasty 3