UniProtKB - H9N289 (NDMA_PSEPU)
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>sp|H9N289|NDMA_PSEPU Methylxanthine N1-demethylase NdmA OS=Pseudomonas putida OX=303 GN=ndmA PE=1 SV=1 MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRD RCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERY GLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPG TLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKY SSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKD APADEVSVVADKVSIQYRKWLRELKEAHKEGSQAFRSALLDPVIESDRSYICommunity curation ()Add a publicationFeedback
Methylxanthine N1-demethylase NdmA
ndmA
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>Select a section on the left to see content.
<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
Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline, paraxanthine, and 1-methylxanthine to 3-methylxanthine, 7-methylxanthine, and xanthine, respectively. NADH is the preferred substrate.
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
<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
- caffeineEC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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- caffeineEC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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- H+EC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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=3-methylxanthine- Search proteins in UniProtKB for this molecule.
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- H+EC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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+theophylline- Search proteins in UniProtKB for this molecule.
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=3-methylxanthine- Search proteins in UniProtKB for this molecule.
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- 1,7-dimethylxanthineEC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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- 1,7-dimethylxanthineEC:1.14.13.178
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
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<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
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<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
<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
- KM=9.1 µM for theophylline (at pH 7.5 and 30 degrees Celsius)2 Publications
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
- KM=37 µM for caffeine (at pH 7.5 and 30 degrees Celsius)2 Publications
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
- KM=53 µM for paraxanthine (at pH 7.5 and 30 degrees Celsius)2 Publications
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
- KM=270 µM for 1-methylxanthine (at pH 7.5 and 30 degrees Celsius)2 Publications
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
pH dependencei
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
Temperature dependencei
Manual assertion based on experiment ini
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.2"Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source."
Summers R.M., Louie T.M., Yu C.L., Subramanian M.
Microbiology 157:583-592(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY.
<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: Alkaloid degradation
This protein is involved in Alkaloid degradation.View all proteins of this organism that are known to be involved in Alkaloid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 bindingi | 62 | Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 64 | Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 81 | Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 84 | Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi | 1 |
<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
- 2 iron, 2 sulfur cluster binding Source: UniProtKB
<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
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
- demethylase activity Source: UniProtKBInferred from direct assayi
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
- metal ion binding Source: UniProtKB-KW
- oxidoreductase activity Source: UniProtKB-KW
GO - Biological processi
- alkaloid catabolic process Source: UniProtKBInferred from direct assayi
- Ref.1"Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids."
Summers R.M., Louie T.M., Yu C.L., Gakhar L., Louie K.C., Subramanian M.
J. Bacteriol. 194:2041-2049(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
<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 function | Oxidoreductase |
Biological process | Alkaloid metabolism |
Ligand | 2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.13.128, 5092 1.14.13.178, 5092 |
<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: Methylxanthine N1-demethylase NdmA (EC:1.14.13.178
Alternative name(s): 1-methylxanthine demethylase |
<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:ndmA |
<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>Organismi | Pseudomonas putida (Arthrobacter siderocapsulatus) |
<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 identifieri | 303 [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 lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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_0000422370 | 1 – 351 | Methylxanthine N1-demethylase NdmAAdd BLAST | 351 |
<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
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 8 – 15 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 16 – 22 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 23 – 29 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 37 – 41 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 44 – 51 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 54 – 61 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 63 – 65 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 69 – 71 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 72 – 75 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 78 – 80 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 82 – 84 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 92 – 96 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 100 – 103 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 113 – 119 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 122 – 127 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 140 – 143 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 148 – 151 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 155 – 159 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 161 – 168 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 171 – 173 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 174 – 177 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 179 – 182 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 185 – 187 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 196 – 198 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 201 – 207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 221 – 228 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 229 – 231 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 232 – 239 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 240 – 242 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 245 – 256 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 259 – 269 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 275 – 295 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 21 | |
Beta strandi | 297 – 300 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 309 – 311 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 312 – 330 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
Helixi | 332 – 340 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 |
3D structure databases
Small Angle Scattering Biological Data Bank More...SASBDBi | H9N289 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | H9N289 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Domaini | 17 – 125 | RieskePROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 109 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.102.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR017941, Rieske_2Fe-2S IPR036922, Rieske_2Fe-2S_sf IPR044043, VanA_C_cat |
Pfam protein domain database More...Pfami | View protein in Pfam PF00355, Rieske, 1 hit PF19112, VanA_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50022, SSF50022, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51296, RIESKE, 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.
10 20 30 40 50
MEQAIINDER EYLRHFWHPV CTVTELEKAH PSSLGPLAVK LLNEQLVVAK
60 70 80 90 100
LGDEYVAMRD RCAHRSAKLS LGTVSGNRLQ CPYHGWQYDT HGACQLVPAC
110 120 130 140 150
PNSPIPNKAK VDRFDCEERY GLIWIRLDSS FDCTEIPYFS AANDPRLRIV
160 170 180 190 200
IQEPYWWDAT AERRWENFTD FSHFAFIHPG TLFDPNNAEP PIVPMDRFNG
210 220 230 240 250
QFRFVYDTPE DMAVPNQAPI GSFSYTCSMP FAINLEVSKY SSSSLHVLFN
260 270 280 290 300
VSCPVDSHTT KNFLIFAREQ SDDSDYLHIA FNDLVFAEDK PVIESQWPKD
310 320 330 340 350
APADEVSVVA DKVSIQYRKW LRELKEAHKE GSQAFRSALL DPVIESDRSY
I
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | JQ061127 Genomic DNA Translation: AFD03116.1 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:AFD03116 |
<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
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
H9N289 | Methylxanthine N1-demethylase | 351 | UniRef100_H9N289 | |||
+1 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
H9N289 | Methylxanthine N1-demethylase | 351 | UniRef90_H9N289 | |||
Rieske domain-containing protein | 351 | |||||
Methylxanthine N1-demethylase | 351 | |||||
Methylxanthine N1-demethylase (Fragment) | 300 | |||||
Methylxanthine N1-demethylase (Fragment) | 134 | |||||
+6 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
H9N289 | Methylxanthine N3-demethylase NdmB | ) | 355 | UniRef50_H9N289 | ||
Methylxanthine N1-demethylase | 351 | |||||
Rieske domain-containing protein | 351 | |||||
Methylxanthine N1-demethylase (Fragment) | 300 | |||||
Methylxanthine N1-demethylase (Fragment) | 134 | |||||
+89 |
<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 | JQ061127 Genomic DNA Translation: AFD03116.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6ICK | X-ray | 1.95 | A/B/C | 1-351 | [»] | |
6ICM | X-ray | 2.96 | A/B/C | 1-351 | [»] | |
6ICN | X-ray | 1.65 | A/B/C | 1-351 | [»] | |
6ICO | X-ray | 1.85 | A/B/C | 1-351 | [»] | |
6ICP | X-ray | 2.20 | A/B/C | 1-351 | [»] | |
6ICQ | X-ray | 1.90 | A/B/C | 1-351 | [»] | |
SASBDBi | H9N289 | |||||
SMRi | H9N289 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
KEGGi | ag:AFD03116 |
Enzyme and pathway databases
BRENDAi | 1.14.13.128, 5092 1.14.13.178, 5092 |
Family and domain databases
Gene3Di | 2.102.10.10, 1 hit |
InterProi | View protein in InterPro IPR017941, Rieske_2Fe-2S IPR036922, Rieske_2Fe-2S_sf IPR044043, VanA_C_cat |
Pfami | View protein in Pfam PF00355, Rieske, 1 hit PF19112, VanA_C, 1 hit |
SUPFAMi | SSF50022, SSF50022, 1 hit |
PROSITEi | View protein in PROSITE PS51296, RIESKE, 1 hit |
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 namei | NDMA_PSEPU | |
<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>Accessioni | H9N289Primary (citable) accession number: H9N289 | |
<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 historyi | Integrated into UniProtKB/Swiss-Prot: | May 29, 2013 |
Last sequence update: | June 13, 2012 | |
Last modified: | February 23, 2022 | |
This is version 30 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic 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, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references