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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
  1. Vmax=44.6 µmol/min/mg enzyme with 2-aminophenol as substrate2 Publications
  2. Vmax=19.0 µmol/min/mg enzyme with 2-aminophenol as substrate2 Publications
  3. Vmax=19.3 µmol/min/mg enzyme with 2-amino-5-chlorophenol as substrate2 Publications
  4. Vmax=1.12 µmol/min/mg enzyme with catechol as substrate2 Publications

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
Metal bindingi13Iron1 Publication1
Metal bindingi62Iron1 Publication1
Metal bindingi251Iron1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.74. 1590.
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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004227811 – 3122-aminophenol 1,6-dioxygenase subunit betaAdd BLAST312

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi16 – 19Combined sources4
Helixi35 – 51Combined sources17
Beta strandi54 – 72Combined sources19
Beta strandi75 – 82Combined sources8
Turni87 – 89Combined sources3
Beta strandi91 – 98Combined sources8
Helixi100 – 112Combined sources13
Beta strandi117 – 120Combined sources4
Helixi129 – 138Combined sources10
Beta strandi146 – 153Combined sources8
Helixi154 – 157Combined sources4
Helixi160 – 181Combined sources22
Beta strandi184 – 189Combined sources6
Helixi208 – 210Combined sources3
Helixi216 – 231Combined sources16
Helixi234 – 248Combined sources15
Helixi251 – 254Combined sources4
Helixi256 – 263Combined sources8
Beta strandi272 – 279Combined sources8
Beta strandi282 – 290Combined sources9
Helixi291 – 294Combined sources4
Beta strandi298 – 301Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK15059.

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8G → E AA sequence (PubMed:15580337).1 Publication1

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.
KEGGiag:AAT35226.
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
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...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6386597.
KEGGiag:AAT35226.
PATRICi35260682. VBIComTes153857_0054.

Phylogenomic databases

KOiK15059.

Enzyme and pathway databases

UniPathwayiUPA00923.
UPA01033.
BRENDAi1.13.11.74. 1590.

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...

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 30, 2016
This is version 41 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

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 one 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.