NADH-quinone oxidoreductase chain 1 - Paracoccus denitrificans

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Reviewed, UniProtKB/Swiss-Prot P29913 (NQO1_PARDE)

Last modified October 13, 2009. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase chain 1
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I, chain 1
    NDH-1, chain 1

Gene names

Name:

nqo1

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic activity	NADH + quinone = NAD⁺ + quinol.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Subunit structure	NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

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Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 431

431

NADH-quinone oxidoreductase chain 1

PRO_0000118566

Regions

Nucleotide binding

54 – 63

NAD By similarity

Nucleotide binding

167 – 214

FMN By similarity

Sites

Metal binding

346

Iron-sulfur (4Fe-4S) Potential

Metal binding

349

Iron-sulfur (4Fe-4S) Potential

Metal binding

352

Iron-sulfur (4Fe-4S) Potential

Metal binding

392

Iron-sulfur (4Fe-4S) Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

P29913-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: AA25C5A0A7570048
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FASTA

431

47,191

        10         20         30         40         50         60 
MLNDQDRIFT NLYGMGDRSL AGAKKRGHWD GTAAIIQRGR DKIIDEMKAS GLRGRGGAGF 

        70         80         90        100        110        120 
PTGMKWSFMP KESDGRPSYL VINADESEPA TCKDREIMRH DPHTLIEGAL IASFAMGAHA 

       130        140        150        160        170        180 
AYIYIRGEFI REREALQAAI DECYDAGLLG RNAAGSGWDF DLYLHHGAGA YICGEETALL 

       190        200        210        220        230        240 
ESLEGKKGMP RMKPPFPAGA GLYGCPTTVN NVESIAVVPT ILRRGAEWFA SFGRPNNAGV 

       250        260        270        280        290        300 
KLFGLTGHVN TPCVVEEAMS IPMRELIEKH GGGIRGGWKN LKAVIPGGAS CPVLTAEQCE 

       310        320        330        340        350        360 
NAIMDYDGMR DVRSSFGTAC MIVMDQSTDV VKAIWRLSKF FKHESCGQCT PCREGTGWMM 

       370        380        390        400        410        420 
RVMERLVRGD AEVEEIDMLF DVTKQVEGHT ICALGDAAAW PIQGLIRNFR EEIEDRIKAK 

       430 
RTGRMGAMAA E

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References

[1]	"The NADH-binding subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: gene cloning and deduced primary structure." Xu X., Matsuno-Yagi A., Yagi T. Biochemistry 30:6422-6428(1991) [PubMed: 1905152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-37. Strain: ATCC 13543 / NRRL B-3784.
[2]	"Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I." Xu X., Matsuno-Yagi A., Yagi T. Biochemistry 30:8678-8684(1991) [PubMed: 1909571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, PROTEIN SEQUENCE OF 1-37 AND 194-203. Strain: ATCC 13543 / NRRL B-3784.
[3]	"Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans." Xu X., Matsuno-Yagi A., Yagi T. Arch. Biochem. Biophys. 296:40-48(1992) [PubMed: 1605643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 416-431.

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Cross-references

Sequence databases
	M64432 Genomic DNA. Translation: AAA25585.1.
PIR	A39588.
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	3.D.1.2.1. proton-translocating NADH dehydrogenase (NDH) family.
Enzyme and pathway databases
BRENDA	1.6.99.5. 59.
Family and domain databases
InterPro	IPR001949. NADH-UbQ_OxRdtase_51kDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011537. NADH-UbQ_OxRdtase_suF. IPR011538. NADH_UbQ_OxRdtase_51kDa_su. IPR019554. Soluble_ligand_bd. [Graphical view]
Pfam	PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
TIGRFAMs	TIGR01959. nuoF_fam. 1 hit.
PROSITE	PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

NQO1_PARDE

Accession

Primary (citable) accession number: P29913

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents