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Protein

1,2-dihydroxynaphthalene dioxygenase

Gene

doxG

Organism
Pseudomonas sp. (strain C18)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the naphthalene catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid (By similarity).By similarity

Catalytic activityi

Naphthalene-1,2-diol + O2 = 2-hydroxy-2H-chromene-2-carboxylate.

Cofactori

Fe2+1 Publication

Pathwayi: naphthalene degradation

This protein is involved in the pathway naphthalene degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway naphthalene degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi152 – 1521Iron
Binding sitei152 – 1521Substrate
Metal bindingi215 – 2151Iron
Binding sitei215 – 2151Substrate
Binding sitei256 – 2561Substrate
Metal bindingi266 – 2661Iron

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

UniPathwayiUPA00082.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-dihydroxynaphthalene dioxygenase (EC:1.13.11.56)
Short name:
1,2-DHN dioxygenase
Short name:
DHNDO
Alternative name(s):
1,2-dihydroxynaphthalene oxygenase
Gene namesi
Name:doxG
Encoded oniPlasmid unnamed1 Publication
OrganismiPseudomonas sp. (strain C18)
Taxonomic identifieri69011 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3023021,2-dihydroxynaphthalene dioxygenasePRO_0000085023Add
BLAST

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi20 – 2910Combined sources
Beta strandi34 – 363Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi54 – 607Combined sources
Beta strandi63 – 7412Combined sources
Helixi75 – 8713Combined sources
Helixi97 – 1037Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi118 – 1258Combined sources
Helixi146 – 1483Combined sources
Beta strandi152 – 1554Combined sources
Helixi160 – 16910Combined sources
Beta strandi176 – 1816Combined sources
Beta strandi187 – 19913Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi210 – 22213Combined sources
Helixi223 – 23513Combined sources
Beta strandi240 – 2467Combined sources
Turni248 – 2503Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi262 – 2698Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi294 – 2963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHZX-ray1.35A1-302[»]
2EI0X-ray1.60A1-302[»]
2EI1X-ray1.52A1-302[»]
2EI2X-ray1.69A1-302[»]
2EI3X-ray1.90A1-302[»]
ProteinModelPortaliP0A108.
SMRiP0A108. Positions 4-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A108.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 2002Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQAAVIEL GYMGISVKDP DAWKSFATDM LGLQVLDEGE KDRFYLRMDY
60 70 80 90 100
WHHRIVVHHN GQDDLEYLGW RVAGKPEFEA LGQKLIDAGY KIRICDKVEA
110 120 130 140 150
QERMVLGLMK TEDPGGNPTE IFWGPRIDMS NPFHPGRPLH GKFVTGDQGL
160 170 180 190 200
GHCIVRQTDV AEAHKFYSLL GFRGDVEYRI PLPNGMTAEL SFMHCNARDH
210 220 230 240 250
SIAFGAMPAA KRLNHLMLEY THMEDLGYTH QQFVKNEIDI ALQLGIHAND
260 270 280 290 300
KALTFYGATP SGWLIEPGWR GATAIDEAEY YVGDIFGHGV EATGYGLDVK

LS
Length:302
Mass (Da):33,942
Last modified:March 1, 2005 - v1
Checksum:iC2A3DAECFB6FB833
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60405 Genomic DNA. Translation: AAA16130.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60405 Genomic DNA. Translation: AAA16130.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHZX-ray1.35A1-302[»]
2EI0X-ray1.60A1-302[»]
2EI1X-ray1.52A1-302[»]
2EI2X-ray1.69A1-302[»]
2EI3X-ray1.90A1-302[»]
ProteinModelPortaliP0A108.
SMRiP0A108. Positions 4-302.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00082.

Miscellaneous databases

EvolutionaryTraceiP0A108.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
PROSITEiPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway."
    Denome S.A., Stanley D.C., Olson E.S., Young K.D.
    J. Bacteriol. 175:6890-6901(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C18.
    Plasmid: unnamed
  2. "Structural explanation for success and failure in the enzymatic ring-cleavage of 3,4 dihydroxybiphenyl and related PCB metabolites."
    Neau D.B., Kelker M.S., Maaroufi H., Colbert C.L., Eltis L.D., Bolin J.T.
    Submitted (MAR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-302 IN COMPLEX WITH SUBSTRATE ANALOGS AND IRON ION, COFACTOR.

Entry informationi

Entry nameiNAHC_PSEU8
AccessioniPrimary (citable) accession number: P0A108
Secondary accession number(s): Q57145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: October 14, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Encoded on an unnamed 75 kb plasmid.1 Publication

Keywords - Technical termi

3D-structure, 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.