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Protein

Cyclomaltodextrin glucanotransferase

Gene

amyA

Organism
Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Status
Reviewed-Annotation score: 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

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54Calcium 11
Metal bindingi56Calcium 1; via carbonyl oxygen1
Metal bindingi59Calcium 11
Metal bindingi60Calcium 11
Metal bindingi78Calcium 1; via carbonyl oxygen1
Metal bindingi80Calcium 11
Metal bindingi167Calcium 21
Binding sitei168SubstrateBy similarity1
Metal bindingi218Calcium 2; via carbonyl oxygen1
Metal bindingi227Calcium 21
Binding sitei255SubstrateBy similarity1
Active sitei257Nucleophile1 Publication1
Metal bindingi261Calcium 2; via carbonyl oxygen1
Active sitei285Proton donor1 Publication1
Binding sitei355SubstrateBy similarity1
Sitei356Transition state stabilizerBy similarity1
Binding sitei398Substrate1
Binding sitei402Substrate1

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. 1534.
SABIO-RKP26827.

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000000144428 – 710Cyclomaltodextrin glucanotransferaseAdd BLAST683

Structurei

Secondary structure

1710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 46Combined sources3
Helixi49 – 51Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 65Combined sources3
Helixi81 – 89Combined sources9
Helixi94 – 96Combined sources3
Beta strandi100 – 103Combined sources4
Beta strandi107 – 109Combined sources3
Beta strandi114 – 116Combined sources3
Turni117 – 119Combined sources3
Beta strandi120 – 122Combined sources3
Beta strandi129 – 136Combined sources8
Turni138 – 140Combined sources3
Helixi143 – 155Combined sources13
Beta strandi159 – 164Combined sources6
Beta strandi168 – 171Combined sources4
Turni180 – 183Combined sources4
Beta strandi185 – 187Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi211 – 213Combined sources3
Helixi214 – 219Combined sources6
Beta strandi220 – 222Combined sources3
Beta strandi225 – 228Combined sources4
Helixi233 – 248Combined sources16
Beta strandi253 – 257Combined sources5
Helixi259 – 261Combined sources3
Helixi264 – 277Combined sources14
Beta strandi281 – 284Combined sources4
Helixi295 – 303Combined sources9
Beta strandi304 – 309Combined sources6
Helixi311 – 321Combined sources11
Helixi328 – 341Combined sources14
Helixi345 – 347Combined sources3
Beta strandi355 – 357Combined sources3
Helixi367 – 378Combined sources12
Beta strandi379 – 386Combined sources8
Helixi389 – 391Combined sources3
Helixi400 – 402Combined sources3
Helixi413 – 421Combined sources9
Helixi424 – 427Combined sources4
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
Beta strandi502 – 504Combined 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 strandi564 – 568Combined sources5
Beta strandi570 – 576Combined sources7
Beta strandi582 – 590Combined sources9
Beta strandi600 – 605Combined sources6
Beta strandi607 – 619Combined sources13
Beta strandi627 – 634Combined sources8
Helixi635 – 637Combined sources3
Turni638 – 640Combined sources3
Helixi642 – 644Combined sources3
Beta strandi652 – 655Combined sources4
Beta strandi659 – 667Combined sources9
Beta strandi671 – 682Combined sources12
Beta strandi684 – 686Combined sources3
Beta strandi692 – 695Combined sources4
Beta strandi698 – 700Combined sources3
Beta strandi702 – 707Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A47X-ray2.56A28-710[»]
1CIUX-ray2.30A28-710[»]
3BMVX-ray1.60A28-710[»]
3BMWX-ray1.60A28-710[»]
ProteinModelPortaliP26827.
SMRiP26827.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini526 – 603IPT/TIGAdd BLAST78
Domaini605 – 710CBM20PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni128 – 129Substrate binding2
Regioni221 – 224Substrate bindingBy similarity4
Regioni260 – 261Substrate binding2

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.
InterProiIPR031319. 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. 3 hits.
PfamiPF00128. Alpha-amylase. 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

        10         20         30         40         50
MKKTFKLILV LMLSLTLVFG LTAPIQAASD TAVSNVVNYS TDVIYQIVTD
60 70 80 90 100
RFVDGNTSNN PTGDLYDPTH TSLKKYFGGD WQGIINKIND GYLTGMGVTA
110 120 130 140 150
IWISQPVENI YAVLPDSTFG GSTSYHGYWA RDFKRTNPYF GSFTDFQNLI
160 170 180 190 200
NTAHAHNIKV IIDFAPNHTS PASETDPTYA ENGRLYDNGT LLGGYTNDTN
210 220 230 240 250
GYFHHYGGTD FSSYEDGIYR NLFDLADLNQ QNSTIDSYLK SAIKVWLDMG
260 270 280 290 300
IDGIRLDAVK HMPFGWQKNF MDSILSYRPV FTFGEWFLGT NEIDVNNTYF
310 320 330 340 350
ANESGMSLLD FRFSQKVRQV FRDNTDTMYG LDSMIQSTAS DYNFINDMVT
360 370 380 390 400
FIDNHDMDRF YNGGSTRPVE QALAFTLTSR GVPAIYYGTE QYMTGNGDPY
410 420 430 440 450
NRAMMTSFNT STTAYNVIKK LAPLRKSNPA IAYGTTQQRW INNDVYIYER
460 470 480 490 500
KFGNNVALVA INRNLSTSYN ITGLYTALPA GTYTDVLGGL LNGNSISVAS
510 520 530 540 550
DGSVTPFTLS AGEVAVWQYV SSSNSPLIGH VGPTMTKAGQ TITIDGRGFG
560 570 580 590 600
TTSGQVLFGS TAGTIVSWDD TEVKVKVPSV TPGKYNISLK TSSGATSNTY
610 620 630 640 650
NNINILTGNQ ICVRFVVNNA STVYGENVYL TGNVAELGNW DTSKAIGPMF
660 670 680 690 700
NQVVYQYPTW YYDVSVPAGT TIQFKFIKKN GNTITWEGGS NHTYTVPSSS
710
TGTVIVNWQQ
Length:710
Mass (Da):78,417
Last modified:February 1, 1996 - v2
Checksum:iF5260AE60D3F27D2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128Missing no nucleotide entry (PubMed:1874408).Curated1
Sequence conflicti133 – 138FKRTNP → LREQS no nucleotide entry (PubMed:1874408).Curated6
Sequence conflicti390 – 398EQYMTGNGD → VYDRQWR AA sequence (PubMed:1854207).Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57692 Genomic DNA. Translation: AAB00845.1.
PIRiS63598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57692 Genomic DNA. Translation: AAB00845.1.
PIRiS63598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A47X-ray2.56A28-710[»]
1CIUX-ray2.30A28-710[»]
3BMVX-ray1.60A28-710[»]
3BMWX-ray1.60A28-710[»]
ProteinModelPortaliP26827.
SMRiP26827.
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. 1534.
SABIO-RKP26827.

Miscellaneous databases

EvolutionaryTraceiP26827.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR031319. 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. 3 hits.
PfamiPF00128. Alpha-amylase. 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_THETU
AccessioniPrimary (citable) accession number: P26827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 124 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

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.