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Protein

Naphthalene 1,2-dioxygenase subunit beta

Gene

ndoC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. The beta subunit may be responsible for the substrate specificity of the enzyme.

Catalytic activityi

Naphthalene + NADH + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+.

Cofactori

Protein has several cofactor binding sites:

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12803.
BRENDAi1.14.12.12. 5092.
UniPathwayiUPA00082.

Names & Taxonomyi

Protein namesi
Recommended name:
Naphthalene 1,2-dioxygenase subunit beta (EC:1.14.12.12)
Alternative name(s):
Naphthalene 1,2-dioxygenase ISP beta
Gene namesi
Name:ndoC
Synonyms:nahAD
Encoded oniPlasmid pDTG11 Publication
Plasmid NAH71 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000850721 – 194Naphthalene 1,2-dioxygenase subunit betaAdd BLAST194

Interactioni

Subunit structurei

The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (NdoR) and ferredoxin (NdoA), and ISP is composed of a hexamer of three large alpha subunits (NdoB) and three small beta subunits (NdoC).

Binary interactionsi

WithEntry#Exp.IntActNotes
ndoBP0A1107EBI-1029028,EBI-1029015

Protein-protein interaction databases

IntActiP0A112. 1 interactor.
MINTiMINT-257448.

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 7Combined sources3
Helixi13 – 23Combined sources11
Helixi28 – 46Combined sources19
Helixi50 – 57Combined sources8
Beta strandi58 – 69Combined sources12
Beta strandi84 – 90Combined sources7
Helixi92 – 103Combined sources12
Helixi108 – 110Combined sources3
Beta strandi115 – 127Combined sources13
Beta strandi134 – 147Combined sources14
Turni148 – 150Combined sources3
Beta strandi151 – 167Combined sources17
Beta strandi170 – 179Combined sources10
Beta strandi183 – 185Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG9X-ray1.60B1-194[»]
1NDOX-ray2.25B/D/F1-194[»]
1O7GX-ray1.70B1-194[»]
1O7HX-ray2.20B1-194[»]
1O7MX-ray1.75B1-194[»]
1O7NX-ray1.40B1-194[»]
1O7PX-ray1.95B1-194[»]
1O7WX-ray1.90B1-194[»]
1UUVX-ray1.65B1-194[»]
1UUWX-ray2.30B1-194[»]
ProteinModelPortaliP0A112.
SMRiP0A112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A112.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMINIQEDKL VSAHDAEEIL RFFNCHDSAL QQEATTLLTQ EAHLLDIQAY
60 70 80 90 100
RAWLEHCVGS EVQYQVISRE LRAASERRYK LNEAMNVYNE NFQQLKVRVE
110 120 130 140 150
HQLDPQNWGN SPKLRFTRFI TNVQAAMDVN DKELLHIRSN VILHRARRGN
160 170 180 190
QVDVFYAARE DKWKRGEGGV RKLVQRFVDY PERILQTHNL MVFL
Length:194
Mass (Da):22,935
Last modified:March 1, 2005 - v1
Checksum:i168D2E1535E66416
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti17E → Q in strain: G7. 1
Natural varianti19I → F in strain: G7. 1
Natural varianti28S → A in strain: G7. 1
Natural varianti39 – 40TQ → NR in strain: G7. 2
Natural varianti99V → I in strain: G7. 1
Natural varianti109G → S in strain: G7. 1
Natural varianti127M → R in strain: G7. 1
Natural varianti130N → D in strain: G7. 1
Natural varianti132K → E in strain: G7. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23914 Genomic DNA. Translation: AAB47592.1.
U49496 Genomic DNA. Translation: AAA92142.1.
M83949 Genomic DNA. Translation: AAA25903.1.
PIRiJN0645.
JS0072.
RefSeqiNP_863073.1. NC_004999.1.
WP_011117401.1. NC_004999.1.
WP_011475378.1. NC_007926.1.
YP_534823.1. NC_007926.1.

Genome annotation databases

GeneIDi1343188.
3974210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23914 Genomic DNA. Translation: AAB47592.1.
U49496 Genomic DNA. Translation: AAA92142.1.
M83949 Genomic DNA. Translation: AAA25903.1.
PIRiJN0645.
JS0072.
RefSeqiNP_863073.1. NC_004999.1.
WP_011117401.1. NC_004999.1.
WP_011475378.1. NC_007926.1.
YP_534823.1. NC_007926.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG9X-ray1.60B1-194[»]
1NDOX-ray2.25B/D/F1-194[»]
1O7GX-ray1.70B1-194[»]
1O7HX-ray2.20B1-194[»]
1O7MX-ray1.75B1-194[»]
1O7NX-ray1.40B1-194[»]
1O7PX-ray1.95B1-194[»]
1O7WX-ray1.90B1-194[»]
1UUVX-ray1.65B1-194[»]
1UUWX-ray2.30B1-194[»]
ProteinModelPortaliP0A112.
SMRiP0A112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A112. 1 interactor.
MINTiMINT-257448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1343188.
3974210.

Enzyme and pathway databases

UniPathwayiUPA00082.
BioCyciMetaCyc:MONOMER-12803.
BRENDAi1.14.12.12. 5092.

Miscellaneous databases

EvolutionaryTraceiP0A112.

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNDOC_PSEPU
AccessioniPrimary (citable) accession number: P0A112
Secondary accession number(s): P23095, Q52125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 30, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.