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P43379

- CDGT2_BACCI

UniProt

P43379 - CDGT2_BACCI

Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus circulans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    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-SubCell

    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

    MKKFLKSTAA LALGLSLTFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD    50
    RFSDGNPANN PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA 100
    IWISQPVENI YSIINYSGVN NTAYHGYWAR DFKKTNPAYG TIADFQNLIA 150
    AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE NGRLYDNGTL LGGYTNDTQN 200
    LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDVYLKD AIKMWLDLGI 250
    DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVSPENHKFA 300
    NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF 350
    IDNHDMERFH ASNANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGTDPD 400
    NRARIPSFST STTAYQVIQK LAPLRKCNPA IAYGSTQERW INNDVLIYER 450
    KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ GSYNDVLGGL LNGNTLSVGS 500
    GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV TITIDGRGFG 550
    SSKGTVYFGT TAVSGADITS WEDTQIKVKI PAVAGGNYNI KVANAAGTAS 600
    NVYDNFEVLS GDQVSVRFVV NNATTALGQN VYLTGSVSEL GNWDPAKAIG 650
    PMYNQVVYQY PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP 700
    SSGTATINVN WQP 713
    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 1, 2014
    This is version 106 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