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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-Experimental evidence at protein leveli

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

Catalytic activityi

2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde.1 Publication
2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde.1 Publication

Cofactori

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

Enzyme 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

Kineticsi

The Km and Vmax values reported for 2-aminophenol differ between PubMed:15580337 and PubMed:23275161.Curated

  1. KM=0.89 µM for 2-aminophenol2 Publications
  2. KM=17.1 µM for 2-aminophenol2 Publications
  3. KM=0.77 µM for 2-amino-5-chlorophenol2 Publications
  4. KM=6.84 µM for catechol2 Publications
  5. KM=77.5 µM for oxygen (in the presence of 2-aminophenol)2 Publications
  6. KM=58.3 µM for oxygen (in the presence of catechol)2 Publications

Vmax=44.6 µmol/min/mg enzyme with 2-aminophenol as substrate2 Publications

Vmax=19.0 µmol/min/mg enzyme with 2-aminophenol as substrate2 Publications

Vmax=19.3 µmol/min/mg enzyme with 2-amino-5-chlorophenol as substrate2 Publications

Vmax=1.12 µmol/min/mg enzyme with catechol as substrate2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Iron1 Publication
Metal bindingi62 – 621Iron1 Publication
Metal bindingi251 – 2511Iron1 Publication

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. ferrous iron binding Source: InterPro

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00923.
UPA01033.

Names & Taxonomyi

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)
Gene namesi
Name:cnbCbImported
Synonyms:amnBImported
Encoded oniPlasmid pCNB14 Publications
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi62 – 621H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi129 – 1291Y → F: Loss of enzyme activity. 1 Publication
Mutagenesisi195 – 1951H → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi251 – 2511E → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3123122-aminophenol 1,6-dioxygenase subunit betaPRO_0000422781Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi16 – 194Combined sources
Helixi35 – 5117Combined sources
Beta strandi54 – 7219Combined sources
Beta strandi75 – 828Combined sources
Turni87 – 893Combined sources
Beta strandi91 – 988Combined sources
Helixi100 – 11213Combined sources
Beta strandi117 – 1204Combined sources
Helixi129 – 13810Combined sources
Beta strandi146 – 1538Combined sources
Helixi154 – 1574Combined sources
Helixi160 – 18122Combined sources
Beta strandi184 – 1896Combined sources
Helixi208 – 2103Combined sources
Helixi216 – 23116Combined sources
Helixi234 – 24815Combined sources
Helixi251 – 2544Combined sources
Helixi256 – 2638Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi282 – 2909Combined sources
Helixi291 – 2944Combined sources
Beta strandi298 – 3014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VSGX-ray2.40B/D1-312[»]
3VSHX-ray2.70B/D1-312[»]
3VSIX-ray2.50B/D1-312[»]
3VSJX-ray2.30B/D1-312[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LigB/MhpB extradiol dioxygenase family.Sequence Analysis

Family and domain databases

Gene3Di3.40.830.10. 1 hit.
InterProiIPR004183. Xdiol_dOase_suB.
[Graphical view]
PfamiPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMiSSF53213. SSF53213. 1 hit.

Sequencei

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
Checksum:iE05323C35EB8EFA4
GO

Sequence cautioni

The sequence AAT35226.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → E AA sequence (PubMed:15580337)1 Publication

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.

Genome annotation databases

GeneIDi6386597.
PATRICi35260682. VBIComTes153857_0054.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VSGX-ray2.40B/D1-312[»]
3VSHX-ray2.70B/D1-312[»]
3VSIX-ray2.50B/D1-312[»]
3VSJX-ray2.30B/D1-312[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6386597.
PATRICi35260682. VBIComTes153857_0054.

Enzyme and pathway databases

UniPathwayiUPA00923.
UPA01033.

Family and domain databases

Gene3Di3.40.830.10. 1 hit.
InterProiIPR004183. Xdiol_dOase_suB.
[Graphical view]
PfamiPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMiSSF53213. SSF53213. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli."
    Wu J.F., Sun C.W., Jiang C.Y., Liu Z.P., Liu S.J.
    Arch. Microbiol. 183:1-8(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: CNB-11 Publication.
    Plasmid: pCNB1
  2. "Novel partial reductive pathway for 4-chloronitrobenzene and nitrobenzene degradation in Comamonas sp. strain CNB-1."
    Wu J.F., Jiang C.Y., Wang B.J., Ma Y.F., Liu Z.P., Liu S.J.
    Appl. Environ. Microbiol. 72:1759-1765(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY.
    Strain: CNB-11 Publication.
    Plasmid: pCNB1
  3. "Nucleotide sequence of plasmid pCNB1 from Comamonas strain CNB-1 reveals novel genetic organization and evolution for 4-chloronitrobenzene degradation."
    Ma Y.F., Wu J.F., Wang S.Y., Jiang C.Y., Zhang Y., Qi S.W., Liu L., Zhao G.P., Liu S.J.
    Appl. Environ. Microbiol. 73:4477-4483(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY.
    Strain: CNB-11 Publication.
    Plasmid: pCNB1
  4. "Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor."
    Li de F., Zhang J.Y., Hou Y.J., Liu L., Hu Y., Liu S.J., Wang da C., Liu W.
    Acta Crystallogr. D 69:32-43(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND IN COMPLEXES WITH REACTION INTERMEDIATE; PRODUCT; INHIBITOR AND IRON, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM, MUTAGENESIS OF HIS-13; HIS-62; TYR-129; HIS-195 AND GLU-251.
    Strain: CNB-11 Publication.
    Plasmid: pCNB1

Entry informationi

Entry nameiAMNB_COMTE
AccessioniPrimary (citable) accession number: Q6J1Z6
Secondary accession number(s): Q38M41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: June 26, 2013
Last modified: November 26, 2014
This is version 36 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.