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Protein

Naphthalene 1,2-dioxygenase subunit alpha

Gene

nagAc

Organism
Ralstonia sp.
Status
Reviewed-Annotation score: Annotation score: 3 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.2 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity
  • [2Fe-2S] clusterPROSITE-ProRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.PROSITE-ProRule annotation

Pathwayi: naphthalene degradation

This protein is involved in the pathway naphthalene degradation, which is part of Aromatic compound metabolism.1 Publication
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)DescriptionActionsGraphical viewLength
Metal bindingi79Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity1
Metal bindingi81Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity1
Metal bindingi99Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity1
Metal bindingi102Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity1
Metal bindingi206IronBy similarity1
Metal bindingi211IronBy similarity1
Metal bindingi360IronBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00082.

Names & Taxonomyi

Protein namesi
Recommended name:
Naphthalene 1,2-dioxygenase subunit alpha1 PublicationBy similarity (EC:1.14.12.121 Publication)
Alternative name(s):
Naphthalene 1,2-dioxygenase large oxygenase component1 PublicationImported
Gene namesi
Name:nagAcImported
Encoded oniPlasmid pWWU2Imported
OrganismiRalstonia sp.
Taxonomic identifieri54061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004218111 – 447Naphthalene 1,2-dioxygenase subunit alphaAdd BLAST447

Interactioni

Subunit structurei

The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an oxygenase component. The electron transfer component is comprised of a ferredoxin reductase (NagAa) and a ferredoxin (NagAb), and the oxygenase component is formed by a large subunit (NagAc) and a small subunit (NagAd).2 Publications

Structurei

3D structure databases

ProteinModelPortaliO52382.
SMRiO52382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 135RieskePROSITE-ProRule annotationAdd BLAST99

Sequence similaritiesi

Contains 1 Rieske domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O52382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYENLVSEA GLTQKHLIHG DKELFQHELK TIFARNWLFL THDSLIPSPG
60 70 80 90 100
DYVTAKMGVD EVIVSRQNDG SVRAFLNVCR HRGKTLVHAE AGNAKGFVCS
110 120 130 140 150
YHGWGFGSNG ELQSVPFEKE LYGDTIKKKC LGLKEVPRIE SFHGFIYGCF
160 170 180 190 200
DAEAPTLVDY LGDAAWYLEP IFKHSGGLEL VGPPGKVVIK ANWKAPAENF
210 220 230 240 250
VGDAYHVGWT HASSLRSGQS IFTPLAGNAM LPPEGAGLQM TSKYGSGMGV
260 270 280 290 300
LWDGYSGVHS ADLVPEMMAF GGAKQEKLAK EIGDVRARIY RSHLNCTVFP
310 320 330 340 350
NNSILTCSGV FKVWNPIDEN TTEVWTYAIV EKDMPEDLKR RLADAVQRTF
360 370 380 390 400
GPAGFWESDD NDNMETESQN AKKYQSSNSD LIANLGFGKD VYGDECYPGV
410 420 430 440
VAKSAIGETS YRGFYRAYQA HISSSNWAEF ENTSRNWHTE LTKTTDR
Length:447
Mass (Da):49,571
Last modified:June 1, 1998 - v1
Checksum:i4553AAF4B4410ED0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12610.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12610.1.

3D structure databases

ProteinModelPortaliO52382.
SMRiO52382.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00082.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNDOB_RALSP
AccessioniPrimary (citable) accession number: O52382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 66 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

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.