NADH-quinone oxidoreductase chain 2 - Paracoccus denitrificans

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Reviewed, UniProtKB/Swiss-Prot P29914 (NQO2_PARDE)

Last modified June 16, 2009. Version 62. 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 2
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I, chain 2
    NDH-1, chain 2

Gene names

Name:

nqo2

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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Protein attributes

Sequence length	239 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 2Fe-2S 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 24 kDa subunit family.

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Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	2Fe-2S 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	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC electron carrier 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 – 239

239

NADH-quinone oxidoreductase chain 2

PRO_0000118685

Sites

Metal binding

Iron-sulfur (2Fe-2S)

Metal binding

101

Iron-sulfur (2Fe-2S)

Metal binding

137

Iron-sulfur (2Fe-2S)

Metal binding

141

Iron-sulfur (2Fe-2S)

Experimental info

Mutagenesis

C → S: No change in UV-visible and EPR spectra. Ref.2

Mutagenesis

H → A: No change in UV-visible and EPR spectra. Ref.2

Mutagenesis

C → A or S: Alters UV-visible and EPR spectra. Ref.2

Mutagenesis

101

C → A or S: Alters UV-visible and EPR spectra. Ref.2

Mutagenesis

104

C → S: No change in UV-visible and EPR spectra. Ref.2

Mutagenesis

113

C → S: No change in UV-visible and EPR spectra. Ref.2

Mutagenesis

137

C → A or S: Alters UV-visible and EPR spectra. Ref.2

Mutagenesis

141

C → A or S: Alters UV-visible and EPR spectra. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P29914-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 6BF734257D670F41
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FASTA

239

26,122

        10         20         30         40         50         60 
MLRRLSPIQP DSFEFTPANL EWARAQMTKY PEGRQQSAII PVLWRAQEQE GWLSRPAIEY 

        70         80         90        100        110        120 
CADLLGMPYI RALEVATFYF MFQLQPVGSV AHIQICGTTT CMICGAEDLI RVCKEKIAPE 

       130        140        150        160        170        180 
PHALSADGRF SWEEVECLGA CTNAPMAQIG KDFYEDLTVE KLAALIDRFA AGEVPVPGPQ 

       190        200        210        220        230 
NGRFSAEALG GPTALADLKG GEAHNASVAR ALRLGDSIKR IDGTEVPITT PWLATQNGV

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References

[1]

"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], PROTEIN SEQUENCE OF 1-10.
Strain: ATCC 13543 / NRRL B-3784.

[2]

"Identification of amino acid residues associated with the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans."
Yano T., Sled V.D., Ohnishi T., Yagi T.
FEBS Lett. 354:160-164(1994) [PubMed: 7957917] [Abstract]
Cited for: MUTAGENESIS OF CYS-61; HIS-92; CYS-96; CYS-101; CYS-104; CYS-113; CYS-137 AND CYS-141.

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Cross-references

Sequence databases
	M74171 Genomic DNA. Translation: AAA25588.1.
PIR	A40296.
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	IPR002023. NADH_UbQ_OxRdtase_su-24kDa. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR10371. Cmplx1_24kDa. 1 hit.
Pfam	PF01257. Complex1_24kDa. 1 hit. [Graphical view]
PIRSF	PIRSF000216. NADH_DH_24kDa. 1 hit.
ProDom	PD003859. Cmplx1_24kDa. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01958. nuoE_fam. 1 hit.
PROSITE	PS01099. COMPLEX1_24K. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

NQO2_PARDE

Accession

Primary (citable) accession number: P29914

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 62 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

Sites

Experimental info

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