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Protein

Naphthalene 1,2-dioxygenase subunit alpha

Gene

doxB

Organism
Pseudomonas sp. (strain C18)
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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster.By similarity
  • Fe cationBy similarityNote: Binds 1 Fe cation.By similarity

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 bindingi81 – 811Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi83 – 831Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation
Metal bindingi101 – 1011Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi104 – 1041Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation
Metal bindingi208 – 2081IronBy similarity
Metal bindingi213 – 2131IronBy similarity
Metal bindingi362 – 3621IronBy similarity

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 alpha (EC:1.14.12.12)
Alternative name(s):
Naphthalene 1,2-dioxygenase ISP alpha
Gene namesi
Name:doxB
Encoded oniPlasmid unnamed1 Publication
OrganismiPseudomonas sp. (strain C18)
Taxonomic identifieri69011 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Naphthalene 1,2-dioxygenase subunit alphaPRO_0000085054Add
BLAST

Interactioni

Subunit structurei

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 and ferredoxin (DoxA), and ISP is composed of a large alpha subunit (DoxB) and a small beta subunit (DoxD) (Probable).Curated

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Helixi11 – 133Combined sources
Beta strandi15 – 173Combined sources
Helixi18 – 214Combined sources
Helixi24 – 3310Combined sources
Turni34 – 374Combined sources
Beta strandi40 – 445Combined sources
Helixi45 – 473Combined sources
Beta strandi53 – 597Combined sources
Beta strandi62 – 687Combined sources
Beta strandi74 – 807Combined sources
Turni82 – 843Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 1004Combined sources
Turni102 – 1043Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi114 – 1163Combined sources
Helixi120 – 1234Combined sources
Turni124 – 1263Combined sources
Helixi130 – 1323Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi147 – 1526Combined sources
Helixi159 – 1635Combined sources
Helixi166 – 1749Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 19314Combined sources
Helixi196 – 2049Combined sources
Helixi209 – 2124Combined sources
Helixi214 – 2207Combined sources
Helixi225 – 2306Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi249 – 2535Combined sources
Turni257 – 2604Combined sources
Turni263 – 2653Combined sources
Helixi266 – 28419Combined sources
Helixi286 – 2927Combined sources
Beta strandi294 – 3007Combined sources
Turni301 – 3033Combined sources
Beta strandi304 – 3074Combined sources
Turni308 – 3114Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi323 – 33311Combined sources
Helixi338 – 35215Combined sources
Helixi357 – 37216Combined sources
Turni376 – 3805Combined sources
Beta strandi382 – 3843Combined sources
Turni387 – 3904Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi397 – 3993Combined sources
Beta strandi401 – 41010Combined sources
Helixi411 – 42414Combined sources
Helixi429 – 4346Combined sources
Turni435 – 4384Combined sources
Helixi439 – 4446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HMJX-ray1.50A1-449[»]
2HMKX-ray1.65A1-449[»]
2HMLX-ray1.80A1-449[»]
2HMMX-ray1.60A1-449[»]
2HMNX-ray1.70A1-449[»]
2HMOX-ray1.60A1-449[»]
4HJLX-ray1.50A1-446[»]
4HKVX-ray1.65A1-449[»]
4HM0X-ray1.80A1-449[»]
4HM1X-ray1.50A1-449[»]
4HM2X-ray1.60A1-449[»]
4HM3X-ray1.50A1-449[»]
4HM4X-ray1.50A1-449[»]
4HM5X-ray1.50A1-449[»]
4HM6X-ray1.50A1-449[»]
4HM7X-ray1.50A1-449[»]
4HM8X-ray1.30A1-449[»]
ProteinModelPortaliP0A111.
SMRiP0A111. Positions 1-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A111.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 13799RieskePROSITE-ProRule annotationAdd
BLAST

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.

P0A111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYNNKILVS ESGLSQKHLI HGDEELFQHE LKTIFARNWL FLTHDSLIPA
60 70 80 90 100
PGDYVTAKMG IDEVIVSRQN DGSIRAFLNV CRHRGKTLVS VEAGNAKGFV
110 120 130 140 150
CSYHGWGFGS NGELQSVPFE KDLYGESLNK KCLGLKEVAR VESFHGFIYG
160 170 180 190 200
CFDQEAPPLM DYLGDAAWYL EPMFKHSGGL ELVGPPGKVV IKANWKAPAE
210 220 230 240 250
NFVGDAYHVG WTHASSLRSG ESIFSSLAGN AALPPEGAGL QMTSKYGSGM
260 270 280 290 300
GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGDVRAR IYRSHLNCTV
310 320 330 340 350
FPNNSMLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADSVQR
360 370 380 390 400
TFGPAGFWES DDNDNMETAS QNGKKYQSRD SDLLSNLGFG EDVYGDAVYP
410 420 430 440
GVVGKSAIGE TSYRGFYRAY QAHVSSSNWA EFEHASSTWH TELTKTTDR
Length:449
Mass (Da):49,608
Last modified:March 1, 2005 - v1
Checksum:i1FD2F42296B4F7A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60405 Genomic DNA. Translation: AAA16125.1.
PIRiS27632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60405 Genomic DNA. Translation: AAA16125.1.
PIRiS27632.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HMJX-ray1.50A1-449[»]
2HMKX-ray1.65A1-449[»]
2HMLX-ray1.80A1-449[»]
2HMMX-ray1.60A1-449[»]
2HMNX-ray1.70A1-449[»]
2HMOX-ray1.60A1-449[»]
4HJLX-ray1.50A1-446[»]
4HKVX-ray1.65A1-449[»]
4HM0X-ray1.80A1-449[»]
4HM1X-ray1.50A1-449[»]
4HM2X-ray1.60A1-449[»]
4HM3X-ray1.50A1-449[»]
4HM4X-ray1.50A1-449[»]
4HM5X-ray1.50A1-449[»]
4HM6X-ray1.50A1-449[»]
4HM7X-ray1.50A1-449[»]
4HM8X-ray1.30A1-449[»]
ProteinModelPortaliP0A111.
SMRiP0A111. Positions 1-447.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00082.

Miscellaneous databases

EvolutionaryTraceiP0A111.

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_PSEU8
AccessioniPrimary (citable) accession number: P0A111
Secondary accession number(s): O07830
, O33461, P23094, Q52124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: December 9, 2015
This is version 58 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.