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P04830 (CDGT1_PAEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cyclomaltodextrin glucanotransferase
EC=2.4.1.19
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name=CGTase
Gene names
Name:cgtM
OrganismPaenibacillus macerans (Bacillus macerans)
Taxonomic identifier44252 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 calcium ions per subunit By similarity.

Subunit structure

Monomer.

Subcellular location

Secreted By similarity.

Domain

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 similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 1 IPT/TIG domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclomaltodextrin glucanotransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 714687Cyclomaltodextrin glucanotransferase
PRO_0000001434

Regions

Domain527 – 60781IPT/TIG
Domain609 – 714106CBM20
Region28 – 165138A1
Region127 – 1282Substrate binding By similarity
Region166 – 22964B
Region220 – 2234Substrate binding By similarity
Region230 – 434205A2
Region259 – 2602Substrate binding By similarity
Region435 – 52389C
Region524 – 61087D
Region611 – 714104E

Sites

Active site2561Nucleophile By similarity
Active site2851Proton donor By similarity
Metal binding541Calcium 1 By similarity
Metal binding591Calcium 1 By similarity
Metal binding601Calcium 1 By similarity
Metal binding781Calcium 1; via carbonyl oxygen By similarity
Metal binding801Calcium 1 By similarity
Metal binding1661Calcium 2 By similarity
Metal binding2171Calcium 2; via carbonyl oxygen By similarity
Metal binding2261Calcium 2 By similarity
Metal binding2601Calcium 2; via carbonyl oxygen By similarity
Binding site1671Substrate By similarity
Binding site2541Substrate By similarity
Binding site3551Substrate By similarity
Binding site3991Substrate By similarity
Binding site4031Substrate By similarity
Site3561Transition state stabilizer By similarity

Experimental info

Sequence conflict152 – 17423AHAHN…PADRD → LTLITSRSDRLRPQPHVSGR AGT in AAA22298. Ref.2
Sequence conflict183 – 1842GM → AL in AAA22298. Ref.2
Sequence conflict260 – 2612HM → QY in AAA22298. Ref.2
Sequence conflict6431S → T in AAA22298. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P04830 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: F8A9AE794D2F3054

FASTA71476,960
        10         20         30         40         50         60 
MKSRYKRLTS LALSLSMALG ISLPAWASPD TSVDNKVNFS TDVIYQIVTD RFADGDRTNN 

        70         80         90        100        110        120 
PAGDAFSGDR SNLKLYFGGD WQGIIDKIND GYLTGMGVTA LWISQPVENI TSVIKYSGVN 

       130        140        150        160        170        180 
NTSYHGYWAR DFKQTNDAFG DFADFQNLID TAHAHNIKVV IDFAPNHTSP ADRDNPGFAE 

       190        200        210        220        230        240 
NGGMYDNGSL LGAYSNDTAG LFHHNGGTDF STIEDGIYKN LYDLADINHN NNAMDAYFKS 

       250        260        270        280        290        300 
AIDLWLGMGV DGIRFDAVKH MPFGWQKSFV SSIYGGDHPV FTFGEWYLGA DQTDGDNIKF 

       310        320        330        340        350        360 
ANESGMNLLD FEYAQEVREV FRDKTETMKD LYEVLASTES QYDYINNMVT FIDNHDMDRF 

       370        380        390        400        410        420 
QVAGSGTRAT EQALALTLTS RGVPAIYYGT EQYMTGDGDP NNRAMMTSFN TGTTAYKVIQ 

       430        440        450        460        470        480 
ALAPLRKSNP AIAYGTTTER WVNNDVLIIE RKFGSSAALV AINRNSSAAY PISGLLSSLP 

       490        500        510        520        530        540 
AGTYSDVLNG LLNGNSITVG SGGAVTNFTL AAGGTAVWQY TAPETSPAIG NVGPTMGQPG 

       550        560        570        580        590        600 
NIVTIDGRGF GGTAGTVYFG TTAVTGSGIV SWEDTQIKAV IPKVAAGKTG VSVKTSSGTA 

       610        620        630        640        650        660 
SNTFKSFNVL TGDQVTVRFL VNQANTNYGT NVYLVGNAAE LGSWDPNKAI GPMYNQVIAK 

       670        680        690        700        710 
YPSWYYDVSV PAGTKLDFKF IKKGGGTVTW EGGGNHTYTT PASGVGTVTV DWQN

« Hide

References

[1]"Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme."
Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K., Imanaka T.
Appl. Environ. Microbiol. 58:4016-4025(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 7069 / DSM 1574 / IAM 1243 / NBRC 3490 / NRRL B-388.
[2]"Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase gene."
Takano T., Fukuda M., Monma M., Kobayashi S., Kainuma K., Yamane K.
J. Bacteriol. 166:1118-1122(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 7069 / DSM 1574 / IAM 1243 / NBRC 3490 / NRRL B-388.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59045 Genomic DNA. Translation: CAA41773.1.
M12777 Genomic DNA. Translation: AAA22298.1.
PIRALBSGR. S31281.

3D structure databases

ProteinModelPortalP04830.
SMRP04830. Positions 28-713.
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.4.1.19. 670.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. 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_TIG_rcpt.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF49452. CBD_4. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDGT1_PAEMA
AccessionPrimary (citable) accession number: P04830
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1994
Last modified: April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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