UniProtKB - P84887 (AAUA_ALCFA)
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>sp|P84887|AAUA_ALCFA Aralkylamine dehydrogenase light chain OS=Alcaligenes faecalis OX=511 GN=aauA PE=1 SV=1 MRWLDKFGESLSRSVAHKTSRRSVLRSVGKLMVGSAFVLPVLPVARAAGGGGSSSGADHI SLNPDLANEDEVNSCDYWRHCAVDGFLCSCCGGTTTTCPPGSTPSPISWIGTCHNPHDGK DYLISYHDCCGKTACGRCQCNTQTRERPGYEFFLHNDVNWCMANENSTFHCTTSVLVGLA KNCommunity curation ()Add a publicationFeedback
Protein
Aralkylamine dehydrogenase light chain
Gene
aauA
Organism
Alcaligenes faecalis
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>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
Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.7 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"Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases."
Chistoserdov A.Y.
Microbiology 147:2195-2202(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. - Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.4"Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes."
Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.
J. Biol. Chem. 270:4293-4298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS. - Ref.8"Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
Roujeinikova A., Scrutton N.S., Leys D.
J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS. - Ref.9"Atomic description of an enzyme reaction dominated by proton tunneling."
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J., Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.
Science 312:237-241(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
<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
- an aralkylamineEC:1.4.9.2
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Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.5"Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR."
Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.
Biochem. J. 330:1159-1163(1998) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.5"Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR."
Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.
Biochem. J. 330:1159-1163(1998) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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an aralkylamine- Search proteins in UniProtKB for this molecule.
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=an aromatic aldehyde- Search proteins in UniProtKB for this molecule.
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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
tryptophan tryptophylquinone residue
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Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS. - Ref.8"Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
Roujeinikova A., Scrutton N.S., Leys D.
J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS. - Ref.9"Atomic description of an enzyme reaction dominated by proton tunneling."
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J., Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.
Science 312:237-241(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS. - Ref.8"Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
Roujeinikova A., Scrutton N.S., Leys D.
J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS. - Ref.9"Atomic description of an enzyme reaction dominated by proton tunneling."
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J., Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.
Science 312:237-241(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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
Irreversibly inhibited by phenylhydrazine, hydroxylamine, semicarbazide, hydrazine and aminoguanidine. Reversibly inhibited by isonicotinic acid hydrazide (isoniazid) and isonicotinic acid 2-isopropyl hydrazide (iproniazid).1 Publication
Manual assertion based on experiment ini
- Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
<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>Absorptioni
Abs(max)=465 nm3 Publications
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
Kineticsi
The enzyme is substrate inhibited at high substrate concentrations (Ki=1.08 mM for tyramine).1 Publication
Manual assertion based on experiment ini
- Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- KM=5.4 µM for tyramine3 Publications
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
- Vmax=17 µmol/min/mg enzyme3 Publications
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
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 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 sitei | 84 | Substrate2 Publications Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei | 109 | Tryptophylquinone 6'-substrate hemiaminal intermediate | 1 | |
| Active sitei | 128 | Proton acceptor2 Publications Manual assertion based on experiment ini
| 1 | |
| <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>Sitei | 172 | Transition state stabilizer | 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
- amine dehydrogenase activity Source: InterPro
- aralkylamine dehydrogenase (azurin) activity Source: UniProtKB-EC
GO - Biological processi
- amine metabolic process Source: InterPro
<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 | Electron transport, Transport |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-16554 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.4.9.2, 232 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P84887 |
<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: Aralkylamine dehydrogenase light chain (EC:1.4.9.2
Alternative name(s): Aromatic amine dehydrogenase Short name: AADH |
| <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:aauA1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <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 | Alcaligenes faecalis |
| <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 | 511 [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 › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Alcaligenes |
<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
Other locations
- Periplasm 2 Publications
Manual assertion based on experiment ini
- Ref.2"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. - Ref.6"Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating Gram-negative bacteria."
Zhu Z., Sun D., Davidson V.L.
J. Bacteriol. 181:6540-6542(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Periplasm 2 Publications
Other locations
- periplasmic space Source: UniProtKB-SubCell
Keywords - Cellular componenti
Periplasm<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 | DB08649, (1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL DB08767, 2-(4-METHOXYPHENYL)ACETAMIDE DB08652, Indoleacetamide DB08653, Tryptamine |
<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 47 | Tat-type signalPROSITE-ProRule annotation <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
| 47 | |
| <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_0000287911 | 48 – 182 | Aralkylamine dehydrogenase light chainPROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 135 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bondi | 75 ↔ 140 | 3 Publications Manual assertion based on experiment ini
| ||
| Disulfide bondi | 81 ↔ 113 | 3 Publications Manual assertion based on experiment ini
| ||
| Disulfide bondi | 88 ↔ 171 | 3 Publications Manual assertion based on experiment ini
| ||
| Disulfide bondi | 90 ↔ 138 | 3 Publications Manual assertion based on experiment ini
| ||
| Disulfide bondi | 91 ↔ 135 | 3 Publications Manual assertion based on experiment ini
| ||
| Disulfide bondi | 98 ↔ 129 | 3 Publications Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 109 ↔ 160 | Tryptophan tryptophylquinone (Trp-Trp)3 Publications Manual assertion based on experiment ini
| ||
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 109 | Tryptophylquinone3 Publications Manual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 130 ↔ 161 | 3 Publications Manual assertion based on experiment ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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
Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.4 Publications
Manual assertion based on experiment ini
- Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS. - Ref.8"Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
Roujeinikova A., Scrutton N.S., Leys D.
J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS. - Ref.9"Atomic description of an enzyme reaction dominated by proton tunneling."
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J., Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.
Science 312:237-241(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Keywords - PTMi
Disulfide bond, TTQ<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
Heterotetramer of two light and two heavy chains. Binds two azurin molecules per heterotetramer.
5 PublicationsManual assertion based on experiment ini
- Ref.3"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.4"Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes."
Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.
J. Biol. Chem. 270:4293-4298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.7"Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS. - Ref.8"Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
Roujeinikova A., Scrutton N.S., Leys D.
J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS. - Ref.9"Atomic description of an enzyme reaction dominated by proton tunneling."
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J., Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.
Science 312:237-241(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 511.JT27_04310 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| 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 | 60 – 62 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 64 – 66 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 69 – 72 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 78 – 80 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <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 | 84 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 88 – 90 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 95 – 97 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 109 – 114 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <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 | 116 – 118 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 121 – 126 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 128 – 132 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 137 – 141 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 149 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 160 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 164 – 166 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 169 – 172 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 175 – 179 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P84887 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P84887 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 156 – 158 | Substrate-binding2 Publications Manual assertion based on experiment ini
| 3 |
<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 aromatic amine dehydrogenase light chain family.Curated
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502ZHBX, Bacteria |
Database of Orthologous Groups More...OrthoDBi | 1619371at2 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.30.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016008, Amine_DH_Ltc IPR036560, MADH/AADH_L_sf IPR013504, MADH/AADH_Ltc_C_dom IPR006311, TAT_signal |
Pfam protein domain database More...Pfami | View protein in Pfam PF02975, Me-amine-dh_L, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000192, Amine_dh_beta, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57561, SSF57561, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE 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%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.
<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 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.
P84887-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MRWLDKFGES LSRSVAHKTS RRSVLRSVGK LMVGSAFVLP VLPVARAAGG
60 70 80 90 100
GGSSSGADHI SLNPDLANED EVNSCDYWRH CAVDGFLCSC CGGTTTTCPP
110 120 130 140 150
GSTPSPISWI GTCHNPHDGK DYLISYHDCC GKTACGRCQC NTQTRERPGY
160 170 180
EFFLHNDVNW CMANENSTFH CTTSVLVGLA KN
Length:182
Mass (Da):19,652
Last modified:May 15, 2007 - 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:i74BC95478B172A41
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 | AF302652 Genomic DNA No translation available. AM292629 Genomic DNA Translation: CAL23525.1 |
NCBI Reference Sequences More...RefSeqi | WP_021447059.1, NZ_RHXK01000003.1 |
Genome annotation databases
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ag:CAL23525 |
<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 | |
|---|---|---|---|---|---|---|
| P84887 | Aralkylamine dehydrogenase light chain | 182 | UniRef100_P84887 | |||
| Amine dehydrogenase | 182 | |||||
| +2 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P84887 | Aralkylamine dehydrogenase light chain | 182 | UniRef90_P84887 | |||
| Amine dehydrogenase | 182 | |||||
| Amine dehydrogenase | 183 | |||||
| Amine dehydrogenase | 183 | |||||
| Amine dehydrogenase | 182 | |||||
| +8 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P84887 | Aralkylamine dehydrogenase light chain | 182 | UniRef50_P84887 | |||
| Amine dehydrogenase | 182 | |||||
| Amine dehydrogenase | 183 | |||||
| Amine dehydrogenase | 186 | |||||
| Amine dehydrogenase | 184 | |||||
| +345 | ||||||
<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 | AF302652 Genomic DNA No translation available. AM292629 Genomic DNA Translation: CAL23525.1 |
| RefSeqi | WP_021447059.1, NZ_RHXK01000003.1 |
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 |
| 2AGL | X-ray | 1.40 | D/H | 48-182 | [»] | |
| 2AGW | X-ray | 1.45 | D/H | 48-182 | [»] | |
| 2AGX | X-ray | 2.20 | D/H | 48-182 | [»] | |
| 2AGY | X-ray | 1.10 | D/H | 48-182 | [»] | |
| 2AGZ | X-ray | 1.60 | D/H | 48-182 | [»] | |
| 2AH0 | X-ray | 1.45 | D/H | 48-182 | [»] | |
| 2AH1 | X-ray | 1.20 | D/H | 48-182 | [»] | |
| 2H3X | X-ray | 2.50 | B/E | 48-182 | [»] | |
| 2H47 | X-ray | 2.60 | B/E/G/I | 48-182 | [»] | |
| 2HJ4 | X-ray | 1.80 | D/H | 48-182 | [»] | |
| 2HJB | X-ray | 1.85 | D/H | 48-182 | [»] | |
| 2HKM | X-ray | 1.50 | D/H | 48-182 | [»] | |
| 2HKR | X-ray | 1.40 | D/H | 59-180 | [»] | |
| 2HXC | X-ray | 1.45 | D/H | 48-182 | [»] | |
| 2I0R | X-ray | 1.40 | D/H | 59-182 | [»] | |
| 2I0S | X-ray | 1.40 | D/H | 59-182 | [»] | |
| 2I0T | X-ray | 1.35 | D/H | 59-180 | [»] | |
| 2IAA | X-ray | 1.95 | B/E | 48-182 | [»] | |
| 2IUP | X-ray | 1.80 | D/H | 48-182 | [»] | |
| 2IUQ | X-ray | 1.50 | D/H | 48-182 | [»] | |
| 2IUR | X-ray | 1.30 | D/H | 48-182 | [»] | |
| 2IUV | X-ray | 1.55 | D/H | 48-182 | [»] | |
| 2OIZ | X-ray | 1.05 | D/H | 48-182 | [»] | |
| 2OJY | X-ray | 1.60 | D/H | 48-180 | [»] | |
| 2OK4 | X-ray | 1.45 | D/H | 48-182 | [»] | |
| 2OK6 | X-ray | 1.45 | D/H | 48-182 | [»] | |
| 2Q7Q | X-ray | 1.60 | D/H | 59-182 | [»] | |
| SMRi | P84887 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 511.JT27_04310 |
Chemistry databases
| DrugBanki | DB08649, (1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL DB08767, 2-(4-METHOXYPHENYL)ACETAMIDE DB08652, Indoleacetamide DB08653, Tryptamine |
Genome annotation databases
| KEGGi | ag:CAL23525 |
Phylogenomic databases
| eggNOGi | ENOG502ZHBX, Bacteria |
| OrthoDBi | 1619371at2 |
Enzyme and pathway databases
| BioCyci | MetaCyc:MONOMER-16554 |
| BRENDAi | 1.4.9.2, 232 |
| SABIO-RKi | P84887 |
Miscellaneous databases
| EvolutionaryTracei | P84887 |
Family and domain databases
| Gene3Di | 2.60.30.10, 1 hit |
| InterProi | View protein in InterPro IPR016008, Amine_DH_Ltc IPR036560, MADH/AADH_L_sf IPR013504, MADH/AADH_Ltc_C_dom IPR006311, TAT_signal |
| Pfami | View protein in Pfam PF02975, Me-amine-dh_L, 1 hit |
| PIRSFi | PIRSF000192, Amine_dh_beta, 1 hit |
| SUPFAMi | SSF57561, SSF57561, 1 hit |
| PROSITEi | View protein in PROSITE PS51318, TAT, 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 namei | AAUA_ALCFA | |
| <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 | P84887Primary (citable) accession number: P84887 Secondary accession number(s): Q0VKG6 | |
| <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 15, 2007 |
| Last sequence update: | May 15, 2007 | |
| Last modified: | April 7, 2021 | |
| This is version 71 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
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
