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Entry version 101 (12 Aug 2020)
Sequence version 2 (19 Oct 2011)
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Protein

Choline trimethylamine-lyase activating enzyme

Gene

cutD

Organism
Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20))
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

Catalyzes activation of the choline trimethylamine-lyase CutC under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM). Is involved in the anaerobic choline utilization pathway that allows D.alaskensis to grow on choline as a source of carbon and energy.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<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

[4Fe-4S] clusterUniRule annotation1 PublicationNote: Binds 2 [4Fe-4S] clusters (PubMed:24854437). One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable).Curated1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: choline degradation

This protein is involved in the pathway choline degradation, which is part of Amine and polyamine metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway choline degradation and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi31Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotationBy similarity1
Metal bindingi35Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotationBy similarity1
Metal bindingi38Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotationBy similarity1
Metal bindingi57Iron-sulfur 2 (4Fe-4S)UniRule annotationCurated1
Metal bindingi60Iron-sulfur 2 (4Fe-4S)UniRule annotationCurated1
Metal bindingi63Iron-sulfur 2 (4Fe-4S)UniRule annotationCurated1
Metal bindingi99Iron-sulfur 2 (4Fe-4S)UniRule annotationCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei139S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotationBy similarity1
Binding sitei264S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotationBy similarity1

<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 functionOxidoreductase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
DALA207559:G1G52-3075-MONOMER
MetaCyc:MONOMER-17847

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA01069

<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%5Fand%5Ftaxonomy%5Fsection">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:
Choline trimethylamine-lyase activating enzyme1 PublicationUniRule annotation (EC:1.97.1.-UniRule annotation1 Publication)
Alternative name(s):
Choline utilization protein D1 PublicationUniRule annotation
GRE activase CutD1 PublicationUniRule annotation
Glycyl-radical enzyme activating enzyme CutD1 PublicationUniRule annotation
Short name:
GRE activating enzyme CutD1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cutD1 PublicationUniRule annotation
Ordered Locus Names:Dde_3281Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiDesulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20))
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri207559 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002710 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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 describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004356661 – 310Choline trimethylamine-lyase activating enzymeAdd BLAST310

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
207559.Dde_3281

<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

3D structure databases

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

More...
SMRi
Q30W71

Database of comparative protein structure models

More...
ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini17 – 304Radical SAM corePROSITE-ProRule annotationAdd BLAST288
Domaini48 – 774Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
Domaini79 – 1094Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST31

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>Regioni37 – 39S-adenosyl-L-methionine bindingUniRule annotationBy similarity3
Regioni188 – 190S-adenosyl-L-methionine bindingUniRule annotationBy similarity3

<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 organic radical-activating enzymes family.UniRule annotationCurated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1180, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_058969_0_0_7

KEGG Orthology (KO)

More...
KOi
K20037

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02059, Activ_enz_CutD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017896, 4Fe4S_Fe-S-bd
IPR017900, 4Fe4S_Fe_S_CS
IPR013785, Aldolase_TIM
IPR040074, BssD/PflA/YjjW
IPR030905, CutC_activ_rSAM
IPR034457, Organic_radical-activating
IPR012839, Organic_radical_activase
IPR001989, Radical_activat_CS
IPR007197, rSAM

The PANTHER Classification System

More...
PANTHERi
PTHR30352, PTHR30352, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13187, Fer4_9, 1 hit
PF04055, Radical_SAM, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000371, PFL_act_enz, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDG01118, activating_enzymes__group_2, 1 hit
SFLDS00029, Radical_SAM, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04395, cutC_activ_rSAM, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00198, 4FE4S_FER_1, 2 hits
PS51379, 4FE4S_FER_2, 2 hits
PS01087, RADICAL_ACTIVATING, 1 hit
PS51918, RADICAL_SAM, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q30W71-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIERKALIFN IQKYNMYDGP GVRTLVFFKG CPLRCKWCSN PEGQLRQYQV
60 70 80 90 100
LYKENLCVHC GACVPVCPAG VHTISASTLR HGFAEGAQCI GCRRCEDVCP
110 120 130 140 150
SSALAVVGEQ KTISELLEVI EEDRPFYETS GGGVTLGGGE VLMQPEAAVN
160 170 180 190 200
LLAACKQHGI NTAIETCGYA KQEVVMKAAQ YVDLFLYDVK HIDSARHYEL
210 220 230 240 250
TGVRNELILS NLTWLLENKH NVKIRVPLLR GVNDSEDDLR GLVEYLRPYQ
260 270 280 290 300
DYKNFKGIDL LPYHKMGVGK YKQLGWEYPI EGNPALSDAD LERVEACIRK
310
YDFPVSVIRH
Length:310
Mass (Da):34,821
Last modified:October 19, 2011 - v2
<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:iBA334312AA784A52
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
CP000112 Genomic DNA Translation: ABB40075.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABB40075; ABB40075; Dde_3281

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dde:Dde_3281

<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
CP000112 Genomic DNA Translation: ABB40075.2

3D structure databases

SMRiQ30W71
ModBaseiSearch...

Protein-protein interaction databases

STRINGi207559.Dde_3281

Genome annotation databases

EnsemblBacteriaiABB40075; ABB40075; Dde_3281
KEGGidde:Dde_3281

Phylogenomic databases

eggNOGiCOG1180, Bacteria
HOGENOMiCLU_058969_0_0_7
KOiK20037

Enzyme and pathway databases

UniPathwayiUPA01069
BioCyciDALA207559:G1G52-3075-MONOMER
MetaCyc:MONOMER-17847

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_02059, Activ_enz_CutD, 1 hit
InterProiView protein in InterPro
IPR017896, 4Fe4S_Fe-S-bd
IPR017900, 4Fe4S_Fe_S_CS
IPR013785, Aldolase_TIM
IPR040074, BssD/PflA/YjjW
IPR030905, CutC_activ_rSAM
IPR034457, Organic_radical-activating
IPR012839, Organic_radical_activase
IPR001989, Radical_activat_CS
IPR007197, rSAM
PANTHERiPTHR30352, PTHR30352, 1 hit
PfamiView protein in Pfam
PF13187, Fer4_9, 1 hit
PF04055, Radical_SAM, 1 hit
PIRSFiPIRSF000371, PFL_act_enz, 1 hit
SFLDiSFLDG01118, activating_enzymes__group_2, 1 hit
SFLDS00029, Radical_SAM, 1 hit
TIGRFAMsiTIGR04395, cutC_activ_rSAM, 1 hit
PROSITEiView protein in PROSITE
PS00198, 4FE4S_FER_1, 2 hits
PS51379, 4FE4S_FER_2, 2 hits
PS01087, RADICAL_ACTIVATING, 1 hit
PS51918, RADICAL_SAM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiCUTD_DESAG
<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: Q30W71
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 16, 2016
Last sequence update: October 19, 2011
Last modified: August 12, 2020
This is version 101 of the entry and version 2 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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