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P26827

- CDGT_THETU

UniProt

P26827 - CDGT_THETU

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Protein
Cyclomaltodextrin glucanotransferase
Gene
amyA
Organism
Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1681Substrate By similarity
Metal bindingi218 – 2181Calcium 2; via carbonyl oxygen
Metal bindingi227 – 2271Calcium 2
Binding sitei255 – 2551Substrate By similarity
Active sitei257 – 2571Nucleophile1 Publication
Metal bindingi261 – 2611Calcium 2; via carbonyl oxygen
Active sitei285 – 2851Proton donor1 Publication
Binding sitei355 – 3551Substrate By similarity
Sitei356 – 3561Transition state stabilizer By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 Publication
Add
BLAST
Chaini28 – 710683Cyclomaltodextrin glucanotransferase
PRO_0000001444Add
BLAST

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP26827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini526 – 60378IPT/TIG
Add
BLAST
Domaini605 – 710106CBM20
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 IPT/TIG domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281Missing no nucleotide entry 1 Publication
Sequence conflicti133 – 1386FKRTNP → LREQS no nucleotide entry 1 Publication
Sequence conflicti390 – 3989EQYMTGNGD → VYDRQWR AA sequence 1 Publication

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: January 22, 2014
This is version 112 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 (1 Publication) thought to be an alpha-amylase.

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

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