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Protein

Cyclomaltodextrin glucanotransferase

Gene
N/A
Organism
Bacillus circulans
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond. EC:2.4.1.19

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi61Calcium 11
Metal bindingi63Calcium 1; via carbonyl oxygen1
Metal bindingi66Calcium 11
Metal bindingi67Calcium 11
Metal bindingi85Calcium 1; via carbonyl oxygen1
Metal bindingi87Calcium 11
Metal bindingi173Calcium 21
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei174Substrate1
Metal bindingi224Calcium 2; via carbonyl oxygen1
Binding sitei230Substrate1
Metal bindingi233Calcium 21
Binding sitei261SubstrateBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei263NucleophileBy similarity1
Metal bindingi267Calcium 2; via carbonyl oxygen1
Binding sitei267Substrate1
Active sitei291Proton donorBy similarity1
Binding sitei361Substrate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei362Transition state stabilizerBy similarity1
Binding sitei405Substrate1
Binding sitei409Substrate1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.19 649

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cyclomaltodextrin glucanotransferase (EC:2.4.1.19)
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name:
CGTase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus circulans
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1397 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02670 4-Deoxy-Alpha-D-Glucose
DB04319 6-Deoxyglucose
DB01909 Alpha-Cyclodextrin (Cyclohexa-Amylose)
DB02379 Beta-D-Glucose
DB03323 Maltose
DB02394 Oxiranpseudoglucose
DB03198 Thio-Maltohexaose
DB01719 Thio-Maltopentaose

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 34Add BLAST34
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000143035 – 718Cyclomaltodextrin glucanotransferaseAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi77 ↔ 84

Keywords - PTMi

Disulfide bond

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1718
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P30920

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P30920

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30920

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini532 – 612IPT/TIGAdd BLAST81
Domaini613 – 718CBM20PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni35 – 172A1Add BLAST138
Regioni134 – 135Substrate binding2
Regioni173 – 236BAdd BLAST64
Regioni227 – 230Substrate bindingBy similarity4
Regioni237 – 440A2Add BLAST204
Regioni266 – 267Substrate binding2
Regioni441 – 528CAdd BLAST88
Regioni529 – 614DAdd BLAST86
Regioni615 – 718EAdd BLAST104

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 2 hits
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR006311 TAT_signal

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00110 ALPHAAMYLASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51166 CBM20, 1 hit
PS51318 TAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P30920-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV
60 70 80 90 100
IYQVFTDRFL DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF
110 120 130 140 150
SDLGVTALWI SQPVENIFAT INYSGVTNTA YHGYWARDFK KTNPYFGTMA
160 170 180 190 200
DFQNLITTAH AKGIKIVIDF APNHTSPAME TDTSFAENGR LYDNGTLVGG
210 220 230 240 250
YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT IDKYFKDAIK
260 270 280 290 300
LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD
310 320 330 340 350
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ
360 370 380 390 400
VNDQVTFIDN HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL
410 420 430 440 450
TGNGDPDNRA KMPSFSKSTT AFNVISKLAP LRKSNPAIAY GSTQQRWINN
460 470 480 490 500
DVYVYERKFG KSVAVVAVNR NLSTSASITG LSTSLPTGSY TDVLGGVLNG
510 520 530 540 550
NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV MGKPGNVVTI
560 570 580 590 600
DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA
610 620 630 640 650
SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST
660 670 680 690 700
GSTAIGPAFN QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN
710
HTFTTPASGT ATVTVNWQ
Length:718
Mass (Da):78,047
Last modified:July 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE08CF0FE9C98BDA1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X68326 Genomic DNA Translation: CAA48401.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S23674 ALBSGC

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68326 Genomic DNA Translation: CAA48401.1
PIRiS23674 ALBSGC

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CGTX-ray2.00A35-718[»]
1CGUX-ray2.50A35-718[»]
3CGTX-ray2.40A35-718[»]
4CGTX-ray2.60A35-718[»]
5CGTX-ray2.50A35-718[»]
6CGTX-ray2.60A35-718[»]
7CGTX-ray3.00A35-718[»]
8CGTX-ray2.40A35-718[»]
9CGTX-ray2.50A35-718[»]
ProteinModelPortaliP30920
SMRiP30920
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB02670 4-Deoxy-Alpha-D-Glucose
DB04319 6-Deoxyglucose
DB01909 Alpha-Cyclodextrin (Cyclohexa-Amylose)
DB02379 Beta-D-Glucose
DB03323 Maltose
DB02394 Oxiranpseudoglucose
DB03198 Thio-Maltohexaose
DB01719 Thio-Maltopentaose

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

BRENDAi2.4.1.19 649

Miscellaneous databases

EvolutionaryTraceiP30920

Family and domain databases

Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR006311 TAT_signal
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit
PS51318 TAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDGT1_BACCI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P30920
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 5, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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