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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)DescriptionActionsGraphical viewLength
Metal bindingi52Calcium 1By similarity1
Metal bindingi54Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi57Calcium 1By similarity1
Metal bindingi58Calcium 1By similarity1
Metal bindingi76Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi78Calcium 1By similarity1
Metal bindingi161Calcium 2By similarity1
Binding sitei162SubstrateBy similarity1
Metal bindingi212Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi221Calcium 2By similarity1
Binding sitei249SubstrateBy similarity1
Active sitei251NucleophileBy similarity1
Metal bindingi255Calcium 2; via carbonyl oxygenBy similarity1
Active sitei279Proton donorBy similarity1
Binding sitei349SubstrateBy similarity1
Sitei350Transition state stabilizerBy similarity1
Binding sitei393SubstrateBy similarity1
Binding sitei397SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000143830 – 703Cyclomaltodextrin glucanotransferaseAdd BLAST674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 75By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP31746.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini520 – 598IPT/TIGAdd BLAST79
Domaini599 – 703CBM20PROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 160A1Add BLAST131
Regioni122 – 123Substrate bindingBy similarity2
Regioni161 – 224BAdd BLAST64
Regioni215 – 218Substrate bindingBy similarity4
Regioni225 – 428A2Add BLAST204
Regioni254 – 255Substrate bindingBy similarity2
Regioni429 – 516CAdd BLAST88
Regioni517 – 600DAdd BLAST84
Regioni601 – 703EAdd BLAST103

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.
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: October 5, 2016
This is version 99 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.