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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial

Gene

At1g79010

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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). May donate electrons to ubiquinone.By similarity

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi123 – 1231Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi126 – 1261Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi129 – 1291Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi133 – 1331Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi162 – 1621Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi165 – 1651Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi168 – 1681Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi172 – 1721Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. metal ion binding Source: TAIR
  3. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Enzyme and pathway databases

BioCyciARA:AT1G79010-MONOMER.
MetaCyc:AT1G79010-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Gene namesi
Ordered Locus Names:At1g79010
ORF Names:YUP8H12R.37, YUP8H12R_21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G79010.

Subcellular locationi

  1. Mitochondrion 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 222NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrialPRO_0000020016
Transit peptidei1 – ?MitochondrionBy similarity

Proteomic databases

PaxDbiQ42599.
PRIDEiQ42599.

Expressioni

Gene expression databases

GenevestigatoriQ42599.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi29461. 1 interaction.
IntActiQ42599. 2 interactions.
STRINGi3702.AT1G79010.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ42599.
SMRiQ42599. Positions 96-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 143304Fe-4S ferredoxin-type 1Add
BLAST
Domaini153 – 182304Fe-4S ferredoxin-type 2Add
BLAST

Sequence similaritiesi

Belongs to the complex I 23 kDa subunit family.Curated
Contains 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG1143.
HOGENOMiHOG000228289.
InParanoidiQ42599.
KOiK03941.
OMAiCMEMYFR.
PhylomeDBiQ42599.

Family and domain databases

HAMAPiMF_01351. NDH1_NuoI.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR010226. NADH_quinone_OxRdtase_chainI.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01971. NuoI. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q42599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE
60 70 80 90 100
QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFDP KVTINYPFEK
110 120 130 140 150
GPLSPRFRGE HALRRYPTGE ERCIACKLCE AVCPAQAITI EAEEREDGSR
160 170 180 190 200
RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFATETH EELLYDKEKL
210 220
LENGDRWETE IAENLRSESL YR
Length:222
Mass (Da):25,503
Last modified:November 1, 1996 - v1
Checksum:i7C1F2264B0D0631B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84318 mRNA. Translation: CAA59061.1.
AC002986 Genomic DNA. Translation: AAC17054.1.
CP002684 Genomic DNA. Translation: AEE36193.1.
AY048241 mRNA. Translation: AAK82503.1.
AY072622 mRNA. Translation: AAL62013.1.
AK226368 mRNA. Translation: BAE98516.1.
AY088308 mRNA. Translation: AAM65847.1.
PIRiS52380.
RefSeqiNP_178022.1. NM_106551.3.
UniGeneiAt.24660.

Genome annotation databases

EnsemblPlantsiAT1G79010.1; AT1G79010.1; AT1G79010.
GeneIDi844242.
KEGGiath:AT1G79010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84318 mRNA. Translation: CAA59061.1.
AC002986 Genomic DNA. Translation: AAC17054.1.
CP002684 Genomic DNA. Translation: AEE36193.1.
AY048241 mRNA. Translation: AAK82503.1.
AY072622 mRNA. Translation: AAL62013.1.
AK226368 mRNA. Translation: BAE98516.1.
AY088308 mRNA. Translation: AAM65847.1.
PIRiS52380.
RefSeqiNP_178022.1. NM_106551.3.
UniGeneiAt.24660.

3D structure databases

ProteinModelPortaliQ42599.
SMRiQ42599. Positions 96-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29461. 1 interaction.
IntActiQ42599. 2 interactions.
STRINGi3702.AT1G79010.1-P.

Proteomic databases

PaxDbiQ42599.
PRIDEiQ42599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G79010.1; AT1G79010.1; AT1G79010.
GeneIDi844242.
KEGGiath:AT1G79010.

Organism-specific databases

GeneFarmi1821. 140.
TAIRiAT1G79010.

Phylogenomic databases

eggNOGiCOG1143.
HOGENOMiHOG000228289.
InParanoidiQ42599.
KOiK03941.
OMAiCMEMYFR.
PhylomeDBiQ42599.

Enzyme and pathway databases

BioCyciARA:AT1G79010-MONOMER.
MetaCyc:AT1G79010-MONOMER.

Miscellaneous databases

PROiQ42599.

Gene expression databases

GenevestigatoriQ42599.

Family and domain databases

HAMAPiMF_01351. NDH1_NuoI.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR010226. NADH_quinone_OxRdtase_chainI.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01971. NuoI. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 28.5-kDa iron-sulfur protein of mitochondrial complex I is encoded in the nucleus in plants."
    Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L.
    Mol. Gen. Genet. 253:448-454(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. C24.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "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 nameiNDS8A_ARATH
AccessioniPrimary (citable) accession number: Q42599
Secondary accession number(s): Q0WWI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 29, 2015
This is version 129 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.