UniProtKB - P30920 (CDGT1_BACCI)
Protein
Cyclomaltodextrin glucanotransferase
Gene
N/A
Organism
Bacillus circulans
Status
Functioni
Catalytic activityi
- Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond. EC:2.4.1.19
Cofactori
Ca2+Note: Binds 2 calcium ions per subunit.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 61 | Calcium 1 | 1 | |
Metal bindingi | 63 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 66 | Calcium 1 | 1 | |
Metal bindingi | 67 | Calcium 1 | 1 | |
Metal bindingi | 85 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 87 | Calcium 1 | 1 | |
Metal bindingi | 173 | Calcium 2 | 1 | |
Binding sitei | 174 | Substrate | 1 | |
Metal bindingi | 224 | Calcium 2; via carbonyl oxygen | 1 | |
Binding sitei | 230 | Substrate | 1 | |
Metal bindingi | 233 | Calcium 2 | 1 | |
Binding sitei | 261 | SubstrateBy similarity | 1 | |
Active sitei | 263 | NucleophileBy similarity | 1 | |
Metal bindingi | 267 | Calcium 2; via carbonyl oxygen | 1 | |
Binding sitei | 267 | Substrate | 1 | |
Active sitei | 291 | Proton donorBy similarity | 1 | |
Binding sitei | 361 | Substrate | 1 | |
Sitei | 362 | Transition state stabilizerBy similarity | 1 | |
Binding sitei | 405 | Substrate | 1 | |
Binding sitei | 409 | Substrate | 1 |
GO - Molecular functioni
- alpha-amylase activity Source: InterPro
- cyclomaltodextrin glucanotransferase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- starch binding Source: InterPro
GO - Biological processi
- carbohydrate metabolic process Source: InterPro
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 2.4.1.19, 649 |
Protein family/group databases
CAZyi | CBM20, 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 |
Organismi | Bacillus circulans |
Taxonomic identifieri | 1397 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & Biotechi
Chemistry databases
DrugBanki | DB01789, 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene DB02469, 4,6-dideoxy-4-amino-beta-D-glucopyranoside DB01841, 4,6-Dideoxyglucose DB02670, 4-Deoxy-Alpha-D-Glucose DB02120, 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol DB01909, Alpha-Cyclodextrin (Cyclohexa-Amylose) DB03773, alpha-D-quinovopyranose DB02379, Beta-D-Glucose DB03323, Maltose DB02394, Oxiranpseudoglucose DB03198, Thio-Maltohexaose DB01719, Thio-Maltopentaose |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 34 | Add BLAST | 34 | |
ChainiPRO_0000001430 | 35 – 718 | Cyclomaltodextrin glucanotransferaseAdd BLAST | 684 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 77 ↔ 84 |
Keywords - PTMi
Disulfide bondProteomic databases
PRIDEi | P30920 |
Interactioni
Subunit structurei
Monomer.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P30920 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P30920 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 532 – 612 | IPT/TIGAdd BLAST | 81 | |
Domaini | 613 – 718 | CBM20PROSITE-ProRule annotationAdd BLAST | 106 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 35 – 172 | A1Add BLAST | 138 | |
Regioni | 134 – 135 | Substrate binding | 2 | |
Regioni | 173 – 236 | BAdd BLAST | 64 | |
Regioni | 227 – 230 | Substrate bindingBy similarity | 4 | |
Regioni | 237 – 440 | A2Add BLAST | 204 | |
Regioni | 266 – 267 | Substrate binding | 2 | |
Regioni | 441 – 528 | CAdd BLAST | 88 | |
Regioni | 529 – 614 | DAdd BLAST | 86 | |
Regioni | 615 – 718 | EAdd BLAST | 104 |
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
SignalFamily and domain databases
Gene3Di | 2.60.40.10, 2 hits 2.60.40.1180, 1 hit |
InterProi | View 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 IPR006311, TAT_signal |
Pfami | View protein in Pfam PF00128, Alpha-amylase, 1 hit PF02806, Alpha-amylase_C, 1 hit PF00686, CBM_20, 1 hit PF01833, TIG, 1 hit |
PRINTSi | PR00110, ALPHAAMYLASE |
SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 1 hit SM01065, CBM_2, 1 hit |
SUPFAMi | SSF49452, SSF49452, 1 hit SSF51445, SSF51445, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51166, CBM20, 1 hit PS51318, TAT, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P30920-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X68326 Genomic DNA Translation: CAA48401.1 |
PIRi | S23674, ALBSGC |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X68326 Genomic DNA Translation: CAA48401.1 |
PIRi | S23674, ALBSGC |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CGT | X-ray | 2.00 | A | 35-718 | [»] | |
1CGU | X-ray | 2.50 | A | 35-718 | [»] | |
3CGT | X-ray | 2.40 | A | 35-718 | [»] | |
4CGT | X-ray | 2.60 | A | 35-718 | [»] | |
5CGT | X-ray | 2.50 | A | 35-718 | [»] | |
6CGT | X-ray | 2.60 | A | 35-718 | [»] | |
7CGT | X-ray | 3.00 | A | 35-718 | [»] | |
8CGT | X-ray | 2.40 | A | 35-718 | [»] | |
9CGT | X-ray | 2.50 | A | 35-718 | [»] | |
SMRi | P30920 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB01789, 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene DB02469, 4,6-dideoxy-4-amino-beta-D-glucopyranoside DB01841, 4,6-Dideoxyglucose DB02670, 4-Deoxy-Alpha-D-Glucose DB02120, 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol DB01909, Alpha-Cyclodextrin (Cyclohexa-Amylose) DB03773, alpha-D-quinovopyranose DB02379, Beta-D-Glucose DB03323, Maltose DB02394, Oxiranpseudoglucose DB03198, Thio-Maltohexaose DB01719, Thio-Maltopentaose |
Protein family/group databases
CAZyi | CBM20, Carbohydrate-Binding Module Family 20 GH13, Glycoside Hydrolase Family 13 |
Proteomic databases
PRIDEi | P30920 |
Enzyme and pathway databases
BRENDAi | 2.4.1.19, 649 |
Miscellaneous databases
EvolutionaryTracei | P30920 |
Family and domain databases
Gene3Di | 2.60.40.10, 2 hits 2.60.40.1180, 1 hit |
InterProi | View 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 IPR006311, TAT_signal |
Pfami | View protein in Pfam PF00128, Alpha-amylase, 1 hit PF02806, Alpha-amylase_C, 1 hit PF00686, CBM_20, 1 hit PF01833, TIG, 1 hit |
PRINTSi | PR00110, ALPHAAMYLASE |
SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 1 hit SM01065, CBM_2, 1 hit |
SUPFAMi | SSF49452, SSF49452, 1 hit SSF51445, SSF51445, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51166, CBM20, 1 hit PS51318, TAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CDGT1_BACCI | |
Accessioni | P30920Primary (citable) accession number: P30920 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | July 1, 1993 | |
Last modified: | April 7, 2021 | |
This is version 131 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families