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Protein

Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific)

Gene

nagAa

Organism
Ralstonia sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene. Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase component via the ferredoxin NagAb. The electron transport chain from the two systems can use both NADH and NADPH as electron donors at approximately similar rates.2 Publications

Catalytic activityi

2 reduced [2Fe-2S] ferredoxin + NAD(P)+ + H+ = 2 oxidized [2Fe-2S] ferredoxin + NAD(P)H.1 Publication

Cofactori

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

Pathwayi: naphthalene degradation

This protein is involved in the pathway naphthalene degradation, which is part of Aromatic compound metabolism.2 Publications
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 bindingi35 – 351Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi40 – 401Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi43 – 431Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi73 – 731Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, NADP

Enzyme and pathway databases

BRENDAi1.18.1.7. 5275.
UniPathwayiUPA00082.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific) (EC:1.18.1.7)
Alternative name(s):
Ferredoxin reductase NagAa
Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase systems, ferredoxin--NAD(P)(+) reductase component
Short name:
NDO/S5H systems ferredoxin--NAD(P)(+) reductase component
Gene namesi
Name:nagAaImported
Encoded oniPlasmid pWWU2Imported
OrganismiRalstonia sp.
Taxonomic identifieri54061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific)PRO_0000421806Add
BLAST

Interactioni

Subunit structurei

The S5H and NDO multicomponent enzyme systems are 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 (NagG or NagAc) and a small subunit (NagH or NagAd).2 Publications

Structurei

3D structure databases

ProteinModelPortaliO52378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 89892Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini96 – 19398FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O52378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVVEPLNL HLNAETGSTL LDVLRSNEVP ISYSCMSGRC GTCRCRVIAG
60 70 80 90 100
HLRDNGPETG RPQAGKGTYV LACQAVLTED CTIEIPESDE IVVHPARIVK
110 120 130 140 150
GTVTAIDEAT HDIRRLRIKL AKPLEFSPGQ YATVQFTPEC VRPYSMAGLP
160 170 180 190 200
SDAEMEFQIR AVPGGHVSNY VFNELSVGAS VRISGPLGTA YLRRTHTGPM
210 220 230 240 250
LCVGGGTGLA PVLSIVRGAL ESGMSNPIHL YFGVRSEQDI YDEERLHALA
260 270 280 290 300
ARFPNLKVNV VVATGPAGPG RRSGLVTDLI GRDLPNLAGW RAYLCGAPAM
310 320
VEALNLLVAR LGIVPGHIHA DAFYPSGV
Length:328
Mass (Da):35,085
Last modified:June 1, 1998 - v1
Checksum:i36B948E841C2983C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12606.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036940 Genomic DNA. Translation: AAD12606.1.

3D structure databases

ProteinModelPortaliO52378.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00082.
BRENDAi1.18.1.7. 5275.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNAGAA_RALSP
AccessioniPrimary (citable) accession number: O52378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: June 1, 1998
Last modified: September 7, 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

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.