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O22769

- NDUV2_ARATH

UniProt

O22769 - NDUV2_ARATH

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Protein

NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

Gene

At4g02580

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

Binds 1 2Fe-2S cluster.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Iron-sulfur (2Fe-2S)Sequence Analysis
Metal bindingi135 – 1351Iron-sulfur (2Fe-2S)Sequence Analysis
Metal bindingi171 – 1711Iron-sulfur (2Fe-2S)Sequence Analysis
Metal bindingi175 – 1751Iron-sulfur (2Fe-2S)Sequence Analysis

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. NADH dehydrogenase (ubiquinone) activity Source: RefGenome
  3. zinc ion binding Source: TAIR

GO - Biological processi

  1. mitochondrial electron transport, NADH to ubiquinone Source: RefGenome
  2. response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Enzyme and pathway databases

BioCyciARA:AT4G02580-MONOMER.
MetaCyc:AT4G02580-MONOMER.

Protein family/group databases

TCDBi3.D.1.6.3. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Gene namesi
Ordered Locus Names:At4g02580
ORF Names:T10P11.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G02580.

Subcellular locationi

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

GO - Cellular componenti

  1. mitochondrial respiratory chain complex I Source: TAIR
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
BLAST
Chaini36 – 255220NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrialPRO_0000020007Add
BLAST

Proteomic databases

PaxDbiO22769.
PRIDEiO22769.

Expressioni

Gene expression databases

ExpressionAtlasiO22769. baseline and differential.
GenevestigatoriO22769.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiO22769. 2 interactions.
STRINGi3702.AT4G02580.1-P.

Structurei

3D structure databases

ProteinModelPortaliO22769.
SMRiO22769. Positions 49-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I 24 kDa subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1905.
HOGENOMiHOG000257748.
InParanoidiO22769.
KOiK03943.
OMAiHIPHIRV.
PhylomeDBiO22769.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002023. NuoE-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10371. PTHR10371. 1 hit.
PIRSFiPIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01958. nuoE_fam. 1 hit.
PROSITEiPS01099. COMPLEX1_24K. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O22769-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS
60 70 80 90 100
EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLPV SAMNAVAKVI
110 120 130 140 150
EVAPIRVYEV ATFYSMFNRA KVGKYHLLVC GTTPCMIRGS RDIESALLDH
160 170 180 190 200
LGVKRGEVTK DGLFSVGEME CMGCCVNAPM ITVADYSNGS EGYTYNYFED
210 220 230 240 250
VTPEKVVEIV EKLRKGEKPP HGTQNPKRIK CGPEGGNKTL LGEPKPPQFR

DLDAC
Length:255
Mass (Da):28,389
Last modified:November 9, 2004 - v3
Checksum:iBD61E8FEF47FE981
GO

Sequence cautioni

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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT01091.
RefSeqiNP_567244.1. NM_116492.3.
UniGeneiAt.22487.

Genome annotation databases

EnsemblPlantsiAT4G02580.1; AT4G02580.1; AT4G02580.
GeneIDi828130.
KEGGiath:AT4G02580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T01091.
RefSeqi NP_567244.1. NM_116492.3.
UniGenei At.22487.

3D structure databases

ProteinModelPortali O22769.
SMRi O22769. Positions 49-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O22769. 2 interactions.
STRINGi 3702.AT4G02580.1-P.

Protein family/group databases

TCDBi 3.D.1.6.3. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Proteomic databases

PaxDbi O22769.
PRIDEi O22769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G02580.1 ; AT4G02580.1 ; AT4G02580 .
GeneIDi 828130.
KEGGi ath:AT4G02580.

Organism-specific databases

GeneFarmi 1820.
TAIRi AT4G02580.

Phylogenomic databases

eggNOGi COG1905.
HOGENOMi HOG000257748.
InParanoidi O22769.
KOi K03943.
OMAi HIPHIRV.
PhylomeDBi O22769.

Enzyme and pathway databases

BioCyci ARA:AT4G02580-MONOMER.
MetaCyc:AT4G02580-MONOMER.

Miscellaneous databases

PROi O22769.

Gene expression databases

ExpressionAtlasi O22769. baseline and differential.
Genevestigatori O22769.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR002023. NuoE-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
PANTHERi PTHR10371. PTHR10371. 1 hit.
PIRSFi PIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR01958. nuoE_fam. 1 hit.
PROSITEi PS01099. COMPLEX1_24K. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiNDUV2_ARATH
AccessioniPrimary (citable) accession number: O22769
Secondary accession number(s): Q940Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 9, 2004
Last modified: October 29, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3