Q52126 (NDOR_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Naphthalene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component
EC=1.18.1.3

Gene names

Name:	ndoR
Synonyms:	nahA1, nahAA

Encoded on

Plasmid pDTG1 Ref.1
Plasmid NAH7 Ref.1
Plasmid NPL1 Ref.2

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. Transfers electrons from ferredoxin (ndoA) to NADH.
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.
Cofactor	Binds 1 2Fe-2S cluster. FAD. Binds 1 mole of FAD per mole of enzyme.
Pathway	Aromatic compound metabolism; naphthalene degradation.
Subunit structure	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 large alpha subunit (ndoB) and a small beta subunit (ndoC).
Sequence similarities	Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 328	328	Naphthalene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component		PRO_0000167657
Regions
	Domain	1 – 89	89	2Fe-2S ferredoxin-type
	Domain	96 – 193	98	FAD-binding FR-type
Sites
	Metal binding	35	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	40	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	43	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	73	1	Iron-sulfur (2Fe-2S) By similarity
Natural variations
	Natural variant	8	1	N → K in strain: BS202.
	Natural variant	11	1	I → L in strain: G7.
	Natural variant	13	1	P → S in strain: G7.
	Natural variant	16	1	A → P in strain: G7.
	Natural variant	36	1	L → M in strain: G7.
	Natural variant	48	1	I → T in strain: G7.
	Natural variant	58 – 59	2	EN → GS in strain: G7.
	Natural variant	61 – 62	2	QS → LP in strain: G7.
	Natural variant	65	1	T → V in strain: G7.
	Natural variant	67 – 68	2	KQ → EH in strain: G7.
	Natural variant	79	1	G → H in strain: G7.
	Natural variant	85	1	V → I in strain: G7.
	Natural variant	88	1	A → T in strain: G7.
	Natural variant	121	1	S → A in strain: G7.
	Natural variant	195	1	K → N in strain: G7.
	Natural variant	222	1	S → L in strain: G7.
	Natural variant	264	1	T → M in strain: G7.
	Natural variant	270	1	G → S in strain: G7.
	Natural variant	276	1	I → V in strain: G7.
	Natural variant	285	1	L → I in strain: G7.

Sequences

	Sequence		Length	Mass (Da)
	Q52126 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4E6237C85CCDF685	FASTA	328	35,501
	10 20 30 40 50 60 MELLIQPNNR IIPFSAGANL LEVLRENGVA ISYSCLSGRC GTCRCRVIDG SVIDSGAENG 70 80 90 100 110 120 QSNLTDKQYV LACQSVLTGN CAIEVPEADE IVTHPARIIK GTVVAVESPT HDIRRLRVRL 130 140 150 160 170 180 SKPFEFSPGQ YATLQFSPEH ARPYSMAGLP DDQEMEFHIR KVPGGRVTEY VFEHVREGTS 190 200 210 220 230 240 IKLSGPLGTA YLRQKHTGPM LCVGGGTGLA PVLSIVRGAL KSGMTNPILL YFGVRSQQDL 250 260 270 280 290 300 YDAERLHKLA ADHPQLTVHT VIATGPINEG QRAGLITDVI EKDILSLAGW RAYLCGAPAM 310 320 VEALCTVTKH LGISPEHIYA DAFYPGGI

References

[1]	"Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4." Simon M.J., Osslund T.D., Saunders R., Ensley B.D., Suggs S., Harcourt A.A., Suen W.-C., Cruden D.L., Gibson D.T., Zylstra G.J. Gene 127:31-37(1993) [PubMed: 8486285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 9816-4 and ATCC 17485 / DSM 50208 / Stanier 111 / JCM 6158 / Biotype A.
[2]	"Evaluation of strains isolated by growth on naphthalene and biphenyl for hybridization of genes to dioxygenase probes and polychlorinated biphenyl-degrading ability." Pellizari V.H., Bezborodnikov S.G., Quensen J.F. III, Tiedje J.M. Appl. Environ. Microbiol. 62:2053-2058(1996) [PubMed: 8787402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BS202.
[3]	"Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816." Haigler B.E., Gibson D.T. J. Bacteriol. 172:457-464(1990) [PubMed: 2294092] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25, CHARACTERIZATION. Strain: DSM 8368 / NCIMB 9816.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF491307 Genomic DNA. Translation: AAA25904.1. M83949 Genomic DNA. Translation: AAA25900.1. AF010471 Genomic DNA. Translation: AAB62705.1.
PIR	JN0640. JN0642.
RefSeq	NP_863070.1. NC_004999.1. YP_534820.1. NC_007926.1.
3D structure databases
ProteinModelPortal	Q52126.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1343185. 3974207.
Phylogenomic databases
ProtClustDB	CLSK896811.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12800.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR017927. Fd_Rdtase_FAD-bd. IPR001041. Ferredoxin. 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]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDOR_PSEPU

Accession

Primary (citable) accession number: Q52126
Secondary accession number(s): O33460, Q52122

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program