Dimethyl sulfoxide reductase DmsA

<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

Miscellaneous

<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<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] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated
• Mo-bis(molybdopterin guanine dinucleotide)3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity."
    Weiner J.H., MacIsaac D.P., Bishop R.E., Bilous P.T.
    J. Bacteriol. 170:1505-1510(1988) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, COFACTOR.
  • Ref.8

    "Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation."
    Rothery R.A., Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H.
    J. Bacteriol. 177:2057-2063(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: COFACTOR, ACTIVITY REGULATION.
  • Ref.10

    "Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase."
    Rothery R.A., Trieber C.A., Weiner J.H.
    J. Biol. Chem. 274:13002-13009(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: MUTAGENESIS OF CYS-67 AND ARG-106, COFACTOR.
  Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity."
    Weiner J.H., MacIsaac D.P., Bishop R.E., Bilous P.T.
    J. Bacteriol. 170:1505-1510(1988) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, COFACTOR.
  • Ref.8

    "Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation."
    Rothery R.A., Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H.
    J. Bacteriol. 177:2057-2063(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: COFACTOR, ACTIVITY REGULATION.
  • Ref.10

    "Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase."
    Rothery R.A., Trieber C.A., Weiner J.H.
    J. Biol. Chem. 274:13002-13009(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: MUTAGENESIS OF CYS-67 AND ARG-106, COFACTOR.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsⁱ

Sites

<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

• 4 iron, 4 sulfur cluster binding Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • 21357619
• cofactor binding Source: EcoCycInferred from mutant phenotypeⁱ
  • 21357619
• dimethyl sulfoxide reductase activity Source: InterPro
• electron transfer activity Source: EcoCycInferred from mutant phenotypeⁱ
  • 8125918
• molybdenum ion binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • 21873635
• molybdopterin cofactor binding Source: InterPro

GO - Biological processⁱ

• anaerobic respiration Source: EcoCyc <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • 2544558

<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

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

• dimethyl sulfoxide reductase complex Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • 3280546
• intrinsic component of periplasmic side of plasma membrane Source: EcoCycInferred from direct assayⁱ
  • 11929547
• outer membrane-bounded periplasmic space Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • 21873635

Keywords - Cellular componentⁱ

<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

Mutagenesis

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Proteomic databases

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<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

<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

Region

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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.

        10         20         30         40         50
MKTKIPDAVL AAEVSRRGLV KTTAIGGLAM ASSALTLPFS RIAHAVDSAI 
        60         70         80         90        100
PTKSDEKVIW SACTVNCGSR CPLRMHVVDG EIKYVETDNT GDDNYDGLHQ 
       110        120        130        140        150
VRACLRGRSM RRRVYNPDRL KYPMKRVGAR GEGKFERISW EEAYDIIATN 
       160        170        180        190        200
MQRLIKEYGN ESIYLNYGTG TLGGTMTRSW PPGNTLVARL MNCCGGYLNH 
       210        220        230        240        250
YGDYSSAQIA EGLNYTYGGW ADGNSPSDIE NSKLVVLFGN NPGETRMSGG 
       260        270        280        290        300
GVTYYLEQAR QKSNARMIII DPRYTDTGAG REDEWIPIRP GTDAALVNGL 
       310        320        330        340        350
AYVMITENLV DQAFLDKYCV GYDEKTLPAS APKNGHYKAY ILGEGPDGVA 
       360        370        380        390        400
KTPEWASQIT GVPADKIIKL AREIGSTKPA FISQGWGPQR HANGEIATRA 
       410        420        430        440        450
ISMLAILTGN VGINGGNSGA REGSYSLPFV RMPTLENPIQ TSISMFMWTD 
       460        470        480        490        500
AIERGPEMTA LRDGVRGKDK LDVPIKMIWN YAGNCLINQH SEINRTHEIL 
       510        520        530        540        550
QDDKKCELIV VIDCHMTSSA KYADILLPDC TASEQMDFAL DASCGNMSYV 
       560        570        580        590        600
IFNDQVIKPR FECKTIYEMT SELAKRLGVE QQFTEGRTQE EWMRHLYAQS 
       610        620        630        640        650
REAIPELPTF EEFRKQGIFK KRDPQGHHVA YKAFREDPQA NPLTTPSGKI 
       660        670        680        690        700
EIYSQALADI AATWELPEGD VIDPLPIYTP GFESYQDPLN KQYPLQLTGF 
       710        720        730        740        750
HYKSRVHSTY GNVDVLKAAC RQEMWINPLD AQKRGIHNGD KVRIFNDRGE 
       760        770        780        790        800
VHIEAKVTPR MMPGVVALGE GAWYDPDAKR VDKGGCINVL TTQRPSPLAK 
       810 
GNPSHTNLVQ VEKV                                        

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

1. SIMILARITY comments
   Index of protein domains and families
2. Escherichia coli
   Escherichia coli (strain K12): entries and cross-references to EcoGene