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Q9FGI6 (NDUS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Protein EMBRYO DEFECTIVE 1467
Gene names
Name:EMB1467
Ordered Locus Names:At5g37510
ORF Names:MPA22.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length748 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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity.

Catalytic activity

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

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Binds 2 4Fe-4S clusters per subunit By similarity.

Subunit structure

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

Subcellular location

Mitochondrion inner membrane By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity. Ref.5

Sequence similarities

Belongs to the complex I 75 kDa subunit family. UniProtKB Q43644

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence caution

The sequence BAB10668.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Ligand2Fe-2S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

cellular respiration

Inferred from Biological aspect of Ancestor. Source: RefGenome

photorespiration

Traceable author statement PubMed 16407270. Source: TAIR

response to oxidative stress

Inferred from direct assay PubMed 12492832. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

mitochondrial membrane

Inferred from direct assay PubMed 16407270. Source: TAIR

mitochondrial respiratory chain complex I

Inferred from direct assay PubMed 18189341PubMed 20197505. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 11743115PubMed 12492832PubMed 12837548Ref.5PubMed 15276431PubMed 22923678. Source: TAIR

respiratory chain complex I

Inferred from direct assay PubMed 16407270. Source: TAIR

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

electron carrier activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FGI6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity UniProtKB Q43644
Chain34 – 748715NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
PRO_0000019972

Regions

Domain72 – 150792Fe-2S ferredoxin-type
Domain287 – 343574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding1061Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q43644
Metal binding1171Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q43644
Metal binding1201Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q43644
Metal binding1341Iron-sulfur 1 (2Fe-2S) By similarity UniProtKB Q43644
Metal binding1661Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1701Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding1731Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding1791Iron-sulfur 2 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding2181Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding2211Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding2241Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB Q43644
Metal binding2681Iron-sulfur 3 (4Fe-4S) By similarity UniProtKB Q43644

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: C83400F148E73F44

FASTA74881,525
        10         20         30         40         50         60 
MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV 

        70         80         90        100        110        120 
GGARVHFSNP EDAIEVFVDG YAVKVPKGFT VLQACEVAGV DIPRFCYHSR LSIAGNCRMC 

       130        140        150        160        170        180 
LVEVEKSPKP VASCAMPALP GMKIKTDTPI AKKAREGVME FLLMNHPLDC PICDQGGECD 

       190        200        210        220        230        240 
LQDQSMAFGS DRGRFTEMKR SVVDKNLGPL VKTVMTRCIQ CTRCVRFASE VAGVQDLGIL 

       250        260        270        280        290        300 
GRGSGEEIGT YVEKLMTSEL SGNVIDICPV GALTSKPFAF KARNWELKAT ETIDVSDAVG 

       310        320        330        340        350        360 
SNIRVDSRGP EVMRIIPRLN EDINEEWISD KTRFCYDGLK RQRLSDPMIR DSDGRFKAVS 

       370        380        390        400        410        420 
WRDALAVVGD IIHQVKPDEI VGVAGQLSDA ESMMVLKDFV NRMGSDNVWC EGTAAGVDAD 

       430        440        450        460        470        480 
LRYSYLMNTS ISGLENADLF LLIGTQPRVE AAMVNARICK TVRASNAKVG YVGPPAEFNY 

       490        500        510        520        530        540 
DCKHLGTGPD TLKEIAEGRH PFCTALKNAK NPAIIVGAGL FNRTDKNAIL SSVESIAQAN 

       550        560        570        580        590        600 
NVVRPDWNGL NFLLQYAAQA AALDLGLIQQ SAKALESAKF VYLMGADDVN VDKIPKDAFV 

       610        620        630        640        650        660 
VYQGHHGDKA VYRANVILPA SAFTEKEGTY ENTEGFTQQT VPAVPTVGDA RDDWKIVRAL 

       670        680        690        700        710        720 
SEVSGVKLPY NSIEGVRSRI KSVAPNLVHT DEREPAAFGP SLKPECKEAM STTPFQTVVE 

       730        740 
NFYMTNSITR ASKIMAQCSA VLLKKPFV 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
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]"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis."
Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.
Plant Physiol. 127:1694-1710(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 511-523.
Tissue: Leaf and Stem.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025630 Genomic DNA. Translation: BAB10668.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED94200.1.
AY056140 mRNA. Translation: AAL07219.1.
RefSeqNP_568550.1. NM_123110.2.
NP_851103.1. NM_180772.1.
UniGeneAt.25266.
At.67340.

3D structure databases

ProteinModelPortalQ9FGI6.
SMRQ9FGI6. Positions 73-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18980. 1 interaction.
IntActQ9FGI6. 2 interactions.

Protein family/group databases

TCDB3.D.1.6.3. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Proteomic databases

PaxDbQ9FGI6.
PRIDEQ9FGI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G37510.2; AT5G37510.2; AT5G37510. [Q9FGI6-1]
GeneID833729.
KEGGath:AT5G37510.

Organism-specific databases

GeneFarm1809.
TAIRAT5G37510.

Phylogenomic databases

eggNOGCOG1034.
HOGENOMHOG000031442.
InParanoidQ9FGI6.
KOK03934.
OMAMPVMKGM.
PhylomeDBQ9FGI6.
ProtClustDBCLSN2689894.

Enzyme and pathway databases

BioCycARA:AT5G37510-MONOMER.
ARA:GQT-20-MONOMER.
MetaCyc:AT5G37510-MONOMER.

Gene expression databases

GenevestigatorQ9FGI6.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9FGI6.

Entry information

Entry nameNDUS1_ARATH
AccessionPrimary (citable) accession number: Q9FGI6
Secondary accession number(s): Q940B1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names