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Entry version 51 (11 Dec 2019)
Sequence version 2 (26 Jun 2013)
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Protein

2-aminophenol 1,6-dioxygenase subunit beta

Gene

cnbCb

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.2 Publications

Miscellaneous

Not active on 4-methylcatechol, 4-chlorocatechol, 2,4-dihydroxybenzoate, o-nitrophenol, p-nitrophenol or 4-nitrocatechol.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Fe2+2 PublicationsNote: Binds 2 Fe2+ ions per APD complex. The iron ions are bound to the beta subunit.2 Publications

<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

Complete loss of activity in the presence of Ni2+, Co2+, Cd2+, Zn2+ and hydrogen peroxide, however activity with hydrogen peroxide partially restored upon addition of excess ascorbate. Partially inhibited by Fe2+, Mg2+, Ca2+, Mn2+, Cu2+ and also by EDTA, at 2 mM concentration. Total activity inhibited in the presence of catechol or 4-nitrocatechol but completely restored after removal of catechol and addition of 2 mM Fe2+ and 5 mM ascorbate.2 Publications

<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

  1. KM=0.89 µM for 2-aminophenol1 Publication
  2. KM=17.1 µM for 2-aminophenol1 Publication
  3. KM=0.77 µM for 2-amino-5-chlorophenol1 Publication
  4. KM=6.84 µM for catechol1 Publication
  5. KM=77.5 µM for oxygen (in the presence of 2-aminophenol)1 Publication
  6. KM=58.3 µM for oxygen (in the presence of catechol)1 Publication
  1. Vmax=44.6 µmol/min/mg enzyme with 2-aminophenol as substrate1 Publication
  2. Vmax=19.0 µmol/min/mg enzyme with 2-aminophenol as substrate1 Publication
  3. Vmax=19.3 µmol/min/mg enzyme with 2-amino-5-chlorophenol as substrate1 Publication
  4. Vmax=1.12 µmol/min/mg enzyme with catechol as substrate1 Publication

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

This protein is involved in the pathway nitrobenzene degradation, which is part of Xenobiotic degradation.2 Publications
View all proteins of this organism that are known to be involved in the pathway nitrobenzene degradation and in Xenobiotic degradation.

Pathwayi: 4-chloronitrobenzene degradation

This protein is involved in the pathway 4-chloronitrobenzene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway 4-chloronitrobenzene degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi13Iron1 Publication1
Metal bindingi62Iron1 Publication1
Metal bindingi251Iron1 Publication1

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

GO - Biological processi

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

Molecular functionDioxygenase, Oxidoreductase
Biological processAromatic hydrocarbons catabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:MONOMER-13344

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.13.11.74 1590

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

More...
UniPathwayi
UPA00923
UPA01033

<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:
2-aminophenol 1,6-dioxygenase subunit beta1 Publication (EC:1.13.11.74)
Alternative name(s):
2-amino-5-chlorophenol 1,6-dioxygenase subunit betaImported (EC:1.13.11.76)
<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:cnbCbImported
Synonyms:amnBImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pCNB14 Publications
<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>OrganismiComamonas testosteroni (Pseudomonas testosteroni)
<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 identifieri285 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi13H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi62H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi129Y → F: Loss of enzyme activity. 1 Publication1
Mutagenesisi195H → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi251E → A: Loss of enzyme activity. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004227811 – 3122-aminophenol 1,6-dioxygenase subunit betaAdd BLAST312

<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

The APD complex is a heterotetramer of 2 alpha (CnbCa) and 2 beta (CnbCb) subunits.

2 Publications

<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

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q6J1Z6

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

<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 LigB/MhpB extradiol dioxygenase family.Sequence analysis

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K15059

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07372 2A5CPDO_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034943 2A5CPDO_B
IPR004183 Xdiol_dOase_suB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02900 LigB, 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.

Q6J1Z6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQGEIIAGFL APHPPHLVYG ENPPQNEPRS QGGWEVLRWA YERARERLDA
60 70 80 90 100
MKPDVLLVHS PHWITSVGHH FLGVPELSGK SVDPIFPNVF RYDFSLNVDV
110 120 130 140 150
ELAEACAEEG RKAGLVTKMM RNPKFRVDYG TITTLHLIRP QWDIPVVGIS
160 170 180 190 200
ANNSPYYLNT KEGMSEMDVL GKATREAIRK TGRKAVLLAS NTLSHWHFHE
210 220 230 240 250
EPTIPEDMSK EYPATMAGYQ WDIRMIELMR QGKTSEVFKL LPQFIDEAFA
260 270 280 290 300
EVKSGAFTWM HAAMQYPELA AELFGYGTVI GTGNAVMEWD LRKAGLSMLG
310
AADQKQRSAA VA
Length:312
Mass (Da):35,040
Last modified:June 26, 2013 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE05323C35EB8EFA4
GO

<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

The sequence AAT35226 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti8G → E AA sequence (PubMed:15580337).1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY605054 Genomic DNA Translation: AAT35226.1 Different initiation.
EF079106 Genomic DNA Translation: ABB13577.1

NCBI Reference Sequences

More...
RefSeqi
YP_001967698.1, NC_010935.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6386597

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAT35226

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|688245.4.peg.54

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY605054 Genomic DNA Translation: AAT35226.1 Different initiation.
EF079106 Genomic DNA Translation: ABB13577.1
RefSeqiYP_001967698.1, NC_010935.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VSGX-ray2.40B/D1-312[»]
3VSHX-ray2.70B/D1-312[»]
3VSIX-ray2.50B/D1-312[»]
3VSJX-ray2.30B/D1-312[»]
SMRiQ6J1Z6
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

GeneIDi6386597
KEGGiag:AAT35226
PATRICifig|688245.4.peg.54

Phylogenomic databases

KOiK15059

Enzyme and pathway databases

UniPathwayiUPA00923
UPA01033
BioCyciMetaCyc:MONOMER-13344
BRENDAi1.13.11.74 1590

Family and domain databases

CDDicd07372 2A5CPDO_B, 1 hit
InterProiView protein in InterPro
IPR034943 2A5CPDO_B
IPR004183 Xdiol_dOase_suB
PfamiView protein in Pfam
PF02900 LigB, 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 nameiAMNB_COMTE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6J1Z6
Secondary accession number(s): Q38M41
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: June 26, 2013
Last modified: December 11, 2019
This is version 51 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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