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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus circulans
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.19 649
SABIO-RKiP43379

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

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

3D structure databases

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit

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

Similar proteinsi

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-RKiP43379

Miscellaneous databases

EvolutionaryTraceiP43379

Family and domain databases

Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCDGT2_BACCI
AccessioniPrimary (citable) accession number: P43379
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 28, 2018
This is version 119 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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