NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P25708 (NDUV1_BOVIN)

Last modified June 16, 2009. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 51 kDa subunit
    Complex I-51kD
      Short name=CI-51kD
    NADH dehydrogenase flavoprotein 1

Gene names

Name:	NDUFV1
Synonyms:	UQOR1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Hide | Top

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic activity	NADH + ubiquinone = NAD⁺ + ubiquinol. NADH + acceptor = NAD⁺ + reduced acceptor.
Cofactor	Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential.
Subunit structure	Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence similarities	Belongs to the complex I 51 kDa subunit family.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain 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: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 20

Mitochondrion

Chain

21 – 464

444

NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

PRO_0000019975

Regions

Nucleotide binding

87 – 96

NAD(H) By similarity

Nucleotide binding

199 – 247

FMN By similarity

Sites

Metal binding

379

Iron-sulfur (4Fe-4S) Potential

Metal binding

382

Iron-sulfur (4Fe-4S) Potential

Metal binding

385

Iron-sulfur (4Fe-4S) Potential

Metal binding

425

Iron-sulfur (4Fe-4S) Potential

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

104

N6-acetyllysine By similarity

Modified residue

375

N6-acetyllysine By similarity

Experimental info

Sequence conflict

413

W → C in AAA30450. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P25708-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 8ACEC256E026B317
Show »

FASTA

464

50,652

        10         20         30         40         50         60 
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG 

        70         80         90        100        110        120 
DWYKTKEILL KGPDWILGEV KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG 

       130        140        150        160        170        180 
EPGTCKDREI IRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG 

       190        200        210        220        230        240 
LIGKNACGSG YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT 

       250        260        270        280        290        300 
TVANVETVAV SPTICRRGGA WFASFGRERN SGTKLFNISG HVNNPCTVEE EMSVPLKELI 

       310        320        330        340        350        360 
EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALIQAQTGLG TAAVIVMDRS 

       370        380        390        400        410        420 
TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV RGDARPAEID SLWEISKQIE 

       430        440        450        460 
GHTICALGDG AAWPVQGLIR HFRPELEERM QQFAQQHQAR QAAF

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA-derived amino acid sequence of the NADH-binding 51-kDa subunit of the bovine respiratory NADH dehydrogenase reveals striking similarities to a bacterial NAD(+)-reducing hydrogenase." Patel S.D., Aebersold R., Attardi G. Proc. Natl. Acad. Sci. U.S.A. 88:4225-4229(1991) [PubMed: 2034666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase." Pilkington S.J., Skehel J.M., Gennis R.B., Walker J.E. Biochemistry 30:2166-2175(1991) [PubMed: 1900194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Basal ganglia.

Hide | Top

Cross-references

Sequence databases
	M58607 mRNA. Translation: AAA30450.1. M63009 mRNA. Translation: AAA30661.1. Different initiation. BC118304 mRNA. Translation: AAI18305.1.
IPI	IPI00702917.
PIR	A39362.
RefSeq	NP_777233.1.
UniGene	Bt.4072
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	3.D.1.6.1. proton-translocating NADH dehydrogenase (NDH) family.
Genome annotation databases
Ensembl	ENSBTAG00000021776. Bos taurus. [Contig view]
GeneID	287014.
KEGG	bta:287014.
Phylogenomic databases
HOVERGEN	P25708.
OMA	P25708. PCNVEEE.
Enzyme and pathway databases
BRENDA	1.6.5.3. 251. 1.6.99.3. 251.
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...

Hide | Top

Entry information

Entry name

NDUV1_BOVIN

Accession

Primary (citable) accession number: P25708
Secondary accession number(s): Q148I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents