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O22769 (NDUV2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
EC=1.6.5.3
EC=1.6.99.3
Gene names
Ordered Locus Names:At4g02580
ORF Names:T10P11.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 By similarity.

Catalytic activity

NADH + ubiquinone = NAD+ + ubiquinol.

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster Potential.

Subunit structure

Complex I is composed of at least 49 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.

Subcellular location

Mitochondrion inner membrane By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.

Sequence similarities

Belongs to the complex I 24 kDa subunit family.

Sequence caution

The sequence AAC78260.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80751.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion Potential
Chain36 – 255220NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
PRO_0000020007

Sites

Metal binding1301Iron-sulfur (2Fe-2S) Potential
Metal binding1351Iron-sulfur (2Fe-2S) Potential
Metal binding1711Iron-sulfur (2Fe-2S) Potential
Metal binding1751Iron-sulfur (2Fe-2S) Potential

Sequences

Sequence LengthMass (Da)Tools
O22769 [UniParc].

Last modified November 9, 2004. Version 3.
Checksum: BD61E8FEF47FE981

FASTA25528,389
        10         20         30         40         50         60 
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI 

        70         80         90        100        110        120 
LSYYPSNYKQ SAVIPLLDLA QQQNGGWLPV SAMNAVAKVI EVAPIRVYEV ATFYSMFNRA 

       130        140        150        160        170        180 
KVGKYHLLVC GTTPCMIRGS RDIESALLDH LGVKRGEVTK DGLFSVGEME CMGCCVNAPM 

       190        200        210        220        230        240 
ITVADYSNGS EGYTYNYFED VTPEKVVEIV EKLRKGEKPP HGTQNPKRIK CGPEGGNKTL 

       250 
LGEPKPPQFR DLDAC

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC002330 Genomic DNA. Translation: AAC78260.1. Sequence problems.
AL161494 Genomic DNA. Translation: CAB80751.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82198.1.
AY052326 mRNA. Translation: AAK96519.1.
BT001140 mRNA. Translation: AAN64531.1.
IPIIPI00521743.
PIRT01091.
RefSeqNP_567244.1. NM_116492.3.
UniGeneAt.22487.

3D structure databases

ProteinModelPortalO22769.
SMRO22769. Positions 49-218.
ModBaseSearch...

Protein-protein interaction databases

IntActO22769. 2 interactions.
STRING3702.AT4G02580.1-P.

Protein family/group databases

TCDB3.D.1.6.3. H+ or Na+-translocating NADH dehydrogenase (NDH) family.

Proteomic databases

PaxDbO22769.
PRIDEO22769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02580.1; AT4G02580.1; AT4G02580.
GeneID828130.
KEGGath:AT4G02580.

Organism-specific databases

GeneFarm1820.
TAIRAt4g02580.

Phylogenomic databases

eggNOGCOG1905.
HOGENOMHOG000257748.
InParanoidO22769.
KOK03943.
OMAKPGPRNG.
PhylomeDBO22769.
ProtClustDBCLSN2689297.

Enzyme and pathway databases

BioCycARA:AT4G02580-MONOMER.
MetaCyc:AT4G02580-MONOMER.

Gene expression databases

ArrayExpressO22769.
GenevestigatorO22769.
GermOnlineAT4G02580. Arabidopsis thaliana.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002023. 2Fe-2S_Ferredox.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR10371. PTHR10371. 1 hit.
PfamPF01257. Complex1_24kDa. 1 hit.
[Graphical view]
PIRSFPIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMsTIGR01958. nuoE_fam. 1 hit.
PROSITEPS01099. COMPLEX1_24K. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDUV2_ARATH
AccessionPrimary (citable) accession number: O22769
Secondary accession number(s): Q940Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 9, 2004
Last modified: May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents