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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus sp. (strain 1-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Calcium 1By similarity
Metal bindingi54 – 541Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi57 – 571Calcium 1By similarity
Metal bindingi58 – 581Calcium 1By similarity
Metal bindingi76 – 761Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi78 – 781Calcium 1By similarity
Metal bindingi161 – 1611Calcium 2By similarity
Binding sitei162 – 1621SubstrateBy similarity
Metal bindingi212 – 2121Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi221 – 2211Calcium 2By similarity
Binding sitei249 – 2491SubstrateBy similarity
Active sitei251 – 2511NucleophileBy similarity
Metal bindingi255 – 2551Calcium 2; via carbonyl oxygenBy similarity
Active sitei279 – 2791Proton donorBy similarity
Binding sitei349 – 3491SubstrateBy similarity
Sitei350 – 3501Transition state stabilizerBy similarity
Binding sitei393 – 3931SubstrateBy similarity
Binding sitei397 – 3971SubstrateBy similarity

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. 691.

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 sp. (strain 1-1)
Taxonomic identifieri29334 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 703674Cyclomaltodextrin glucanotransferasePRO_0000001438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 75By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP31746.
SMRiP31746. Positions 33-703.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini520 – 59879IPT/TIGAdd
BLAST
Domaini599 – 703105CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 160131A1Add
BLAST
Regioni122 – 1232Substrate bindingBy similarity
Regioni161 – 22464BAdd
BLAST
Regioni215 – 2184Substrate bindingBy similarity
Regioni225 – 428204A2Add
BLAST
Regioni254 – 2552Substrate bindingBy similarity
Regioni429 – 51688CAdd
BLAST
Regioni517 – 60084DAdd
BLAST
Regioni601 – 703103EAdd
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.
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. 2 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.

P31746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDLNDFLKT ILLSFIFFLL LSLPTVAEAD VTNKVNYSKD VIYQIVTDRF
60 70 80 90 100
SDGNPGNNPS GAIFSQNCID LHKYCGGDWQ GIIDKINDGY LTDLGITALW
110 120 130 140 150
ISQPVENVYA LHPSGYTSYH GYWARDYKKT NPYYGNFDDF DRLMSTAHSN
160 170 180 190 200
GIKVIMDFTP NHSSPALETN PNYVENGAIY DNGALLGNYS NDQQNLFHHN
210 220 230 240 250
GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKFW LDKGIDGIRV
260 270 280 290 300
DAVKHMSEGW QTSLMSEIYS HKPVFTFGEW FLGSGEVDPQ NHHFANESGM
310 320 330 340 350
SLLDFQFGQT IRNVLKDRTS NWYDFNEMIT STEKEYNEVI DQVTFIDNHD
360 370 380 390 400
MSRFSVGSSS NRQTDMALAV LLTSRGVPTI YYGTEQYVTG GNDPENRKPL
410 420 430 440 450
KTFDRSTNSY QIISKLASLR QTNSALGYGT TTERWLNEDI YIYERTFGNS
460 470 480 490 500
IVLTAVNSSN SNQTITNLNT SLPQGNYTDE LQQRLDGNTI TVNANGAVNS
510 520 530 540 550
FQLRANSVAV WQVSNPSTSP LIGQVGPMMG KAGNTITVSG EGFGDERGSV
560 570 580 590 600
LFDSTSSEII SWSNTKISVK VPNVAGGYYD LSVVTAANIK SPTYKEFEVL
610 620 630 640 650
SGNQVSVRFG VNNATTSPGT NLYIVGNVNE LGNWDADKAI GPMFNQVMYQ
660 670 680 690 700
YPTWYYDISV PAGKNLEYKY IKKDQNGNVV WQSGNNRTYT SPTTGTDTVM

INW
Length:703
Mass (Da):78,663
Last modified:July 1, 1993 - v1
Checksum:i4D973FB21D0D9B0A
GO

Sequence databases

PIRiS26399. ALBSX1.

Cross-referencesi

Sequence databases

PIRiS26399. ALBSX1.

3D structure databases

ProteinModelPortaliP31746.
SMRiP31746. Positions 33-703.
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. 691.

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. 2 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_BACS2
AccessioniPrimary (citable) accession number: P31746
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 98 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

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.