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P26827

- CDGT_THETU

UniProt

P26827 - CDGT_THETU

Protein

Cyclomaltodextrin glucanotransferase

Gene

amyA

Organism
Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Degrades starch to alpha-, beta-, and gamma-cyclodextrins, as well as linear sugars.

    Catalytic activityi

    Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.

    Cofactori

    Binds 2 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 bindingi167 – 1671Calcium 2
    Binding sitei168 – 1681SubstrateBy similarity
    Metal bindingi218 – 2181Calcium 2; via carbonyl oxygen
    Metal bindingi227 – 2271Calcium 2
    Binding sitei255 – 2551SubstrateBy similarity
    Active sitei257 – 2571Nucleophile1 Publication
    Metal bindingi261 – 2611Calcium 2; via carbonyl oxygen
    Active sitei285 – 2851Proton donor1 Publication
    Binding sitei355 – 3551SubstrateBy similarity
    Sitei356 – 3561Transition state stabilizerBy similarity
    Binding sitei398 – 3981Substrate
    Binding sitei402 – 4021Substrate

    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. 6287.

    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:amyA
    OrganismiThermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
    Taxonomic identifieri33950 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 710683Cyclomaltodextrin glucanotransferasePRO_0000001444Add
    BLAST

    Structurei

    Secondary structure

    1
    710
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 463
    Helixi49 – 513
    Helixi57 – 593
    Helixi63 – 653
    Helixi81 – 899
    Helixi94 – 963
    Beta strandi100 – 1034
    Beta strandi107 – 1093
    Beta strandi114 – 1163
    Turni117 – 1193
    Beta strandi120 – 1223
    Beta strandi129 – 1368
    Turni138 – 1403
    Helixi143 – 15513
    Beta strandi159 – 1646
    Beta strandi168 – 1714
    Turni180 – 1834
    Beta strandi185 – 1873
    Beta strandi190 – 1934
    Beta strandi211 – 2133
    Helixi214 – 2196
    Beta strandi220 – 2223
    Beta strandi225 – 2284
    Helixi233 – 24816
    Beta strandi253 – 2575
    Helixi259 – 2613
    Helixi264 – 27714
    Beta strandi281 – 2844
    Helixi295 – 3039
    Beta strandi304 – 3096
    Helixi311 – 32111
    Helixi328 – 34114
    Helixi345 – 3473
    Beta strandi355 – 3573
    Helixi367 – 37812
    Beta strandi379 – 3868
    Helixi389 – 3913
    Helixi400 – 4023
    Helixi413 – 4219
    Helixi424 – 4274
    Helixi429 – 4335
    Beta strandi435 – 4417
    Beta strandi443 – 45210
    Beta strandi455 – 4628
    Beta strandi469 – 4713
    Beta strandi480 – 4834
    Turni486 – 4916
    Beta strandi496 – 4983
    Beta strandi502 – 5043
    Beta strandi507 – 5093
    Beta strandi514 – 5196
    Beta strandi527 – 5326
    Beta strandi534 – 5363
    Beta strandi541 – 5477
    Beta strandi555 – 5584
    Beta strandi564 – 5685
    Beta strandi570 – 5767
    Beta strandi582 – 5909
    Beta strandi600 – 6056
    Beta strandi607 – 61913
    Beta strandi627 – 6348
    Helixi635 – 6373
    Turni638 – 6403
    Helixi642 – 6443
    Beta strandi652 – 6554
    Beta strandi659 – 6679
    Beta strandi671 – 68212
    Beta strandi684 – 6863
    Beta strandi692 – 6954
    Beta strandi698 – 7003
    Beta strandi702 – 7076

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A47X-ray2.56A28-710[»]
    1CIUX-ray2.30A28-710[»]
    3BMVX-ray1.60A28-710[»]
    3BMWX-ray1.60A28-710[»]
    ProteinModelPortaliP26827.
    SMRiP26827. Positions 28-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26827.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini526 – 60378IPT/TIGAdd
    BLAST
    Domaini605 – 710106CBM20PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni128 – 1292Substrate binding
    Regioni221 – 2244Substrate bindingBy similarity
    Regioni260 – 2612Substrate binding

    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.

    P26827-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTFKLILV LMLSLTLVFG LTAPIQAASD TAVSNVVNYS TDVIYQIVTD    50
    RFVDGNTSNN PTGDLYDPTH TSLKKYFGGD WQGIINKIND GYLTGMGVTA 100
    IWISQPVENI YAVLPDSTFG GSTSYHGYWA RDFKRTNPYF GSFTDFQNLI 150
    NTAHAHNIKV IIDFAPNHTS PASETDPTYA ENGRLYDNGT LLGGYTNDTN 200
    GYFHHYGGTD FSSYEDGIYR NLFDLADLNQ QNSTIDSYLK SAIKVWLDMG 250
    IDGIRLDAVK HMPFGWQKNF MDSILSYRPV FTFGEWFLGT NEIDVNNTYF 300
    ANESGMSLLD FRFSQKVRQV FRDNTDTMYG LDSMIQSTAS DYNFINDMVT 350
    FIDNHDMDRF YNGGSTRPVE QALAFTLTSR GVPAIYYGTE QYMTGNGDPY 400
    NRAMMTSFNT STTAYNVIKK LAPLRKSNPA IAYGTTQQRW INNDVYIYER 450
    KFGNNVALVA INRNLSTSYN ITGLYTALPA GTYTDVLGGL LNGNSISVAS 500
    DGSVTPFTLS AGEVAVWQYV SSSNSPLIGH VGPTMTKAGQ TITIDGRGFG 550
    TTSGQVLFGS TAGTIVSWDD TEVKVKVPSV TPGKYNISLK TSSGATSNTY 600
    NNINILTGNQ ICVRFVVNNA STVYGENVYL TGNVAELGNW DTSKAIGPMF 650
    NQVVYQYPTW YYDVSVPAGT TIQFKFIKKN GNTITWEGGS NHTYTVPSSS 700
    TGTVIVNWQQ 710
    Length:710
    Mass (Da):78,417
    Last modified:February 1, 1996 - v2
    Checksum:iF5260AE60D3F27D2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281Missing no nucleotide entry (PubMed:1874408)Curated
    Sequence conflicti133 – 1386FKRTNP → LREQS no nucleotide entry (PubMed:1874408)Curated
    Sequence conflicti390 – 3989EQYMTGNGD → VYDRQWR AA sequence (PubMed:1854207)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57692 Genomic DNA. Translation: AAB00845.1.
    PIRiS63598.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57692 Genomic DNA. Translation: AAB00845.1 .
    PIRi S63598.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A47 X-ray 2.56 A 28-710 [» ]
    1CIU X-ray 2.30 A 28-710 [» ]
    3BMV X-ray 1.60 A 28-710 [» ]
    3BMW X-ray 1.60 A 28-710 [» ]
    ProteinModelPortali P26827.
    SMRi P26827. Positions 28-710.
    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. 6287.

    Miscellaneous databases

    EvolutionaryTracei P26827.

    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. "Alpha-amylase of Clostridium thermosulfurogenes EM1: nucleotide sequence of the gene, processing of the enzyme, and comparison of other alpha-amylases."
      Bahl H., Burchhardt G., Spreinat A., Haeckel K., Wienecke A., Schmidt B., Antranikian G.
      Appl. Environ. Microbiol. 57:1554-1559(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-48, SUBCELLULAR LOCATION.
      Strain: DSM 3896 / EM1.
    2. Sahm K., Matuschek M., Mueller H., Mitchell W.J., Bahl H.
      Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 3896 / EM1.
    3. "Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding protein-dependent transport systems."
      Bahl H., Burchhardt G., Wienecke A.
      FEMS Microbiol. Lett. 65:83-87(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-255.
      Strain: DSM 3896 / EM1.
    4. "Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase."
      Wind R.D., Liebl W., Buitelaar R.M., Penninga D., Spreinat A., Dijkhuizen L., Bahl H.
      Appl. Environ. Microbiol. 61:1257-1265(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1."
      Knegtel R.M.A., Wind R.D., Rozeboom H.J., Kalk K.H., Buitelaar R.M., Dijkhuizen L., Dijkstra B.W.
      J. Mol. Biol. 256:611-622(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 28-710.
    6. "Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1."
      Wind R.D., Uitdehaag J.C., Buitelaar R.M., Dijkstra B.W., Dijkhuizen L.
      J. Biol. Chem. 273:5771-5779(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 28-710 IN COMPLEX WITH MALTOHEPTAOSE AND CALCIUM IONS.
      Strain: DSM 3896 / EM1.

    Entry informationi

    Entry nameiCDGT_THETU
    AccessioniPrimary (citable) accession number: P26827
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be an alpha-amylase.1 Publication

    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