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Q6J1Z6

- AMNB_COMTE

UniProt

Q6J1Z6 - AMNB_COMTE

Protein

2-aminophenol 1,6-dioxygenase subunit beta

Gene

cnbCb

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 2 (26 Jun 2013)
      Previous versions | rss
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    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

    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

    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 – 109
    Helixi16 – 194
    Helixi35 – 5117
    Beta strandi54 – 7219
    Beta strandi75 – 828
    Turni87 – 893
    Beta strandi91 – 988
    Helixi100 – 11213
    Beta strandi117 – 1204
    Helixi129 – 13810
    Beta strandi146 – 1538
    Helixi154 – 1574
    Helixi160 – 18122
    Beta strandi184 – 1896
    Helixi208 – 2103
    Helixi216 – 23116
    Helixi234 – 24815
    Helixi251 – 2544
    Helixi256 – 2638
    Beta strandi272 – 2798
    Beta strandi282 – 2909
    Helixi291 – 2944
    Beta strandi298 – 3014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MQGEIIAGFL APHPPHLVYG ENPPQNEPRS QGGWEVLRWA YERARERLDA    50
    MKPDVLLVHS PHWITSVGHH FLGVPELSGK SVDPIFPNVF RYDFSLNVDV 100
    ELAEACAEEG RKAGLVTKMM RNPKFRVDYG TITTLHLIRP QWDIPVVGIS 150
    ANNSPYYLNT KEGMSEMDVL GKATREAIRK TGRKAVLLAS NTLSHWHFHE 200
    EPTIPEDMSK EYPATMAGYQ WDIRMIELMR QGKTSEVFKL LPQFIDEAFA 250
    EVKSGAFTWM HAAMQYPELA AELFGYGTVI GTGNAVMEWD LRKAGLSMLG 300
    AADQKQRSAA VA 312
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY605054 Genomic DNA. Translation: AAT35226.1 . Different initiation.
    EF079106 Genomic DNA. Translation: ABB13577.1 .
    RefSeqi YP_001967698.1. NC_010935.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VSG X-ray 2.40 B/D 1-312 [» ]
    3VSH X-ray 2.70 B/D 1-312 [» ]
    3VSI X-ray 2.50 B/D 1-312 [» ]
    3VSJ X-ray 2.30 B/D 1-312 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6386597.
    PATRICi 35260682. VBIComTes153857_0054.

    Enzyme and pathway databases

    UniPathwayi UPA00923 .
    UPA01033 .

    Family and domain databases

    Gene3Di 3.40.830.10. 1 hit.
    InterProi IPR004183. Xdiol_dOase_suB.
    [Graphical view ]
    Pfami PF02900. LigB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53213. SSF53213. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 35 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