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Q6J1Z6 (AMNB_COMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-aminophenol 1,6-dioxygenase subunit beta

EC=1.13.11.74
Alternative name(s):
2-amino-5-chlorophenol 1,6-dioxygenase subunit beta
EC=1.13.11.76
Gene names
Name:cnbCb
Synonyms:amnB
Encoded onPlasmid pCNB1 Ref.1 Ref.2 Ref.3 Ref.4
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde. Ref.1

2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde. Ref.1

Cofactor

Binds 2 Fe2+ ions per APD complex. The iron ions are bound to the beta subunit. Ref.1 Ref.4

Enzyme regulation

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. Ref.1 Ref.4

Pathway

Xenobiotic degradation; nitrobenzene degradation. Ref.2 Ref.3

Xenobiotic degradation; 4-chloronitrobenzene degradation. Ref.2 Ref.3

Subunit structure

The APD complex is a heterotetramer of 2 alpha (CnbCa) and 2 beta (CnbCb) subunits. Ref.1 Ref.4

Miscellaneous

Not active on 4-methylcatechol, 4-chlorocatechol, 2,4-dihydroxybenzoate, o-nitrophenol, p-nitrophenol or 4-nitrocatechol. Ref.1

Sequence similarities

Belongs to the LigB/MhpB extradiol dioxygenase family.

Biophysicochemical properties

Kinetic parameters:

The Km and Vmax values reported for 2-aminophenol differ between Ref.1 and Ref.4.

KM=0.89 µM for 2-aminophenol (Ref.1) Ref.1 Ref.4

KM=17.1 µM for 2-aminophenol (Ref.4)

KM=0.77 µM for 2-amino-5-chlorophenol (Ref.1)

KM=6.84 µM for catechol (Ref.4)

KM=77.5 µM for oxygen (in the presence of 2-aminophenol) (Ref.4)

KM=58.3 µM for oxygen (in the presence of catechol) (Ref.4)

Vmax=44.6 µmol/min/mg enzyme with 2-aminophenol as substrate (Ref.1)

Vmax=19.0 µmol/min/mg enzyme with 2-aminophenol as substrate (Ref.4)

Vmax=19.3 µmol/min/mg enzyme with 2-amino-5-chlorophenol as substrate (Ref.1)

Vmax=1.12 µmol/min/mg enzyme with catechol as substrate (Ref.4)

Sequence caution

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

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ferrous iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3123122-aminophenol 1,6-dioxygenase subunit beta
PRO_0000422781

Sites

Metal binding131Iron Ref.4
Metal binding621Iron Ref.4
Metal binding2511Iron Ref.4

Experimental info

Mutagenesis131H → A: Loss of enzyme activity. Ref.4
Mutagenesis621H → A: Loss of enzyme activity. Ref.4
Mutagenesis1291Y → F: Loss of enzyme activity. Ref.4
Mutagenesis1951H → Q: Loss of enzyme activity. Ref.4
Mutagenesis2511E → A: Loss of enzyme activity. Ref.4
Sequence conflict81G → E AA sequence Ref.1

Secondary structure

............................................. 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6J1Z6 [UniParc].

Last modified June 26, 2013. Version 2.
Checksum: E05323C35EB8EFA4

FASTA31235,040
        10         20         30         40         50         60 
MQGEIIAGFL APHPPHLVYG ENPPQNEPRS QGGWEVLRWA YERARERLDA MKPDVLLVHS 

        70         80         90        100        110        120 
PHWITSVGHH FLGVPELSGK SVDPIFPNVF RYDFSLNVDV ELAEACAEEG RKAGLVTKMM 

       130        140        150        160        170        180 
RNPKFRVDYG TITTLHLIRP QWDIPVVGIS ANNSPYYLNT KEGMSEMDVL GKATREAIRK 

       190        200        210        220        230        240 
TGRKAVLLAS NTLSHWHFHE EPTIPEDMSK EYPATMAGYQ WDIRMIELMR QGKTSEVFKL 

       250        260        270        280        290        300 
LPQFIDEAFA EVKSGAFTWM HAAMQYPELA AELFGYGTVI GTGNAVMEWD LRKAGLSMLG 

       310 
AADQKQRSAA VA 

« Hide

References

[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-1.
[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-1.
[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-1.
[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-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY605054 Genomic DNA. Translation: AAT35226.1. Different initiation.
EF079106 Genomic DNA. Translation: ABB13577.1.
RefSeqYP_001967698.1. NC_010935.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VSGX-ray2.40B/D1-312[»]
3VSHX-ray2.70B/D1-312[»]
3VSIX-ray2.50B/D1-312[»]
3VSJX-ray2.30B/D1-312[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6386597.
PATRIC35260682. VBIComTes153857_0054.

Enzyme and pathway databases

UniPathwayUPA00923.
UPA01033.

Family and domain databases

Gene3D3.40.830.10. 1 hit.
InterProIPR004183. Xdiol_dOase_suB.
[Graphical view]
PfamPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMSSF53213. SSF53213. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMNB_COMTE
AccessionPrimary (citable) accession number: Q6J1Z6
Secondary accession number(s): Q38M41
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: June 26, 2013
Last modified: May 14, 2014
This is version 34 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways