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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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 bindingi55Calcium 11
Metal bindingi57Calcium 1; via carbonyl oxygen1
Metal bindingi60Calcium 11
Metal bindingi61Calcium 11
Metal bindingi79Calcium 1; via carbonyl oxygen1
Metal bindingi81Calcium 11
Metal bindingi166Calcium 21
Binding sitei167SubstrateBy similarity1
Metal bindingi217Calcium 2; via carbonyl oxygen1
Metal bindingi226Calcium 21
Binding sitei254SubstrateBy similarity1
Active sitei256Nucleophile1
Metal bindingi260Calcium 2; via carbonyl oxygen1
Active sitei284Proton donor1
Binding sitei354SubstrateBy similarity1
Sitei355Transition state stabilizerBy similarity1
Binding sitei398SubstrateBy similarity1
Binding sitei402SubstrateBy similarity1

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. 623.

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
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000000144232 – 711Cyclomaltodextrin glucanotransferaseAdd BLAST680

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi71 ↔ 78

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1711
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 48Combined sources4
Helixi50 – 52Combined sources3
Helixi58 – 60Combined sources3
Helixi64 – 66Combined sources3
Helixi69 – 71Combined sources3
Helixi82 – 90Combined sources9
Turni93 – 98Combined sources6
Beta strandi101 – 104Combined sources4
Beta strandi108 – 110Combined sources3
Beta strandi116 – 119Combined sources4
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
Helixi213 – 217Combined sources5
Beta strandi218 – 221Combined sources4
Beta strandi224 – 227Combined sources4
Helixi232 – 246Combined sources15
Turni247 – 249Combined sources3
Beta strandi252 – 256Combined sources5
Helixi258 – 260Combined sources3
Helixi264 – 276Combined sources13
Beta strandi280 – 283Combined sources4
Helixi294 – 302Combined sources9
Beta strandi306 – 308Combined sources3
Helixi310 – 320Combined sources11
Helixi327 – 340Combined sources14
Helixi344 – 346Combined sources3
Helixi367 – 378Combined sources12
Beta strandi379 – 386Combined sources8
Helixi389 – 391Combined sources3
Helixi400 – 402Combined sources3
Helixi413 – 427Combined sources15
Helixi429 – 433Combined sources5
Beta strandi435 – 441Combined sources7
Beta strandi443 – 452Combined sources10
Beta strandi455 – 462Combined sources8
Beta strandi469 – 471Combined sources3
Beta strandi480 – 483Combined sources4
Turni486 – 491Combined sources6
Beta strandi496 – 498Combined sources3
Helixi500 – 502Combined sources3
Beta strandi507 – 509Combined sources3
Beta strandi514 – 519Combined sources6
Beta strandi527 – 532Combined sources6
Beta strandi534 – 536Combined sources3
Beta strandi541 – 547Combined sources7
Beta strandi555 – 558Combined sources4
Beta strandi565 – 567Combined sources3
Beta strandi570 – 576Combined sources7
Beta strandi582 – 590Combined sources9
Beta strandi600 – 605Combined sources6
Beta strandi610 – 619Combined sources10
Beta strandi627 – 634Combined sources8
Helixi635 – 637Combined sources3
Helixi642 – 644Combined sources3
Beta strandi652 – 655Combined sources4
Beta strandi660 – 669Combined sources10
Beta strandi671 – 679Combined sources9
Beta strandi685 – 687Combined sources3
Beta strandi693 – 696Combined sources4
Beta strandi699 – 701Combined sources3
Beta strandi703 – 708Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CYGX-ray2.50A32-711[»]
ProteinModelPortaliP31797.
SMRiP31797.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini526 – 604IPT/TIGAdd BLAST79
Domaini605 – 711CBM20PROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 165A1Add BLAST134
Regioni127 – 128Substrate bindingBy similarity2
Regioni166 – 229BAdd BLAST64
Regioni220 – 223Substrate bindingBy similarity4
Regioni230 – 433A2Add BLAST204
Regioni259 – 260Substrate bindingBy similarity2
Regioni434 – 522CAdd BLAST89
Regioni523 – 606DAdd BLAST84
Regioni607 – 711EAdd BLAST105

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.

P31797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRWLSLVLS MSFVFSAIFI VSDTQKVTVE AAGNLNKVNF TSDVVYQIVV
60 70 80 90 100
DRFVDGNTSN NPSGALFSSG CTNLRKYCGG DWQGIINKIN DGYLTDMGVT
110 120 130 140 150
AIWISQPVEN VFSVMNDASG SASYHGYWAR DFKKPNPFFG TLSDFQRLVD
160 170 180 190 200
AAHAKGIKVI IDFAPNHTSP ASETNPSYME NGRLYDNGTL LGGYTNDANM
210 220 230 240 250
YFHHNGGTTF SSLEDGIYRN LFDLADLNHQ NPVIDRYLKD AVKMWIDMGI
260 270 280 290 300
DGIRMDAVKH MPFGWQKSLM DEIDNYRPVF TFGEWFLSEN EVDANNHYFA
310 320 330 340 350
NESGMSLLDF RFGQKLRQVL RNNSDNWYGF NQMIQDTASA YDEVLDQVTF
360 370 380 390 400
IDNHDMDRFM IDGGDPRKVD MALAVLLTSR GVPNIYYGTE QYMTGNGDPN
410 420 430 440 450
NRKMMSSFNK NTRAYQVIQK LSSLRRNNPA LAYGDTEQRW INGDVYVYER
460 470 480 490 500
QFGKDVVLVA VNRSSSSNYS ITGLFTALPA GTYTDQLGGL LDGNTIQVGS
510 520 530 540 550
NGSVNAFDLG PGEVGVWAYS ATESTPIIGH VGPMMGQVGH QVTIDGEGFG
560 570 580 590 600
TNTGTVKFGT TAANVVSWSN NQIVVAVPNV SPGKYNITVQ SSSGQTSAAY
610 620 630 640 650
DNFEVLTNDQ VSVRFVVNNA TTNLGQNIYI VGNVYELGNW DTSKAIGPMF
660 670 680 690 700
NQVVYSYPTW YIDVSVPEGK TIEFKFIKKD SQGNVTWESG SNHVYTTPTN
710
TTGKIIVDWQ N
Length:711
Mass (Da):78,923
Last modified:July 1, 1993 - v1
Checksum:i5F9F71FF01C2CC60
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti460A → R AA sequence (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59042 Genomic DNA. Translation: CAA41770.1.
X59043 Genomic DNA. Translation: CAA41771.1.
X59044 Genomic DNA. Translation: CAA41772.1.
PIRiS26588. ALBSXF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59042 Genomic DNA. Translation: CAA41770.1.
X59043 Genomic DNA. Translation: CAA41771.1.
X59044 Genomic DNA. Translation: CAA41772.1.
PIRiS26588. ALBSXF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CYGX-ray2.50A32-711[»]
ProteinModelPortaliP31797.
SMRiP31797.
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. 623.

Miscellaneous databases

EvolutionaryTraceiP31797.

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 nameiCDGT_GEOSE
AccessioniPrimary (citable) accession number: P31797
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, 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.