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Q42577 (NDUS7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 121. 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

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Gene names
Ordered Locus Names:At5g11770
ORF Names:T22P22_160
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. HAMAP-Rule MF_01356

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). HAMAP-Rule MF_01356

NADH + acceptor = NAD+ + reduced acceptor. HAMAP-Rule MF_01356

Cofactor

Binds 1 4Fe-4S cluster Potential.

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 Ref.6.

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 218NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial HAMAP-Rule MF_01356PRO_0000020033

Sites

Metal binding931Iron-sulfur (4Fe-4S) Potential
Metal binding941Iron-sulfur (4Fe-4S) Potential
Metal binding1581Iron-sulfur (4Fe-4S) Potential
Metal binding1881Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q42577 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D4FC0E15A4029908

FASTA21824,044
        10         20         30         40         50         60 
MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG 

        70         80         90        100        110        120 
LSKAAEFVIS KVDDLMNWAR TGSIWPMTFG LACCAVEMMH TGAARYDLDR FGIIFRPSPR 

       130        140        150        160        170        180 
QSDCMIVAGT LTNKMAPALR KVYDQMPEPR WVISMGSCAN GGGYYHYSYS VVRGCDRIVP 

       190        200        210 
VDIYVPGCPP TAEALLYGLL QLQKKINRRK DFLHWWNK 

« Hide

References

« Hide 'large scale' references
[1]"The plant mitochondrial 22 kDa (PSST) subunit of respiratory chain complex I is encoded by a nuclear gene with enhanced transcript levels in flowers."
Heiser V., Grohmann L., Brennicke A.
Plant Mol. Biol. 31:1195-1204(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. C24.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(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. 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.
[5]"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].
[6]"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
X84078 mRNA. Translation: CAA58887.1.
AL163814 Genomic DNA. Translation: CAB87695.1.
CP002688 Genomic DNA. Translation: AED91719.1.
AF428300 mRNA. Translation: AAL16132.1.
AY056182 mRNA. Translation: AAL07031.1.
AY099848 mRNA. Translation: AAM20699.1.
AY128912 mRNA. Translation: AAM91312.1.
AY085120 mRNA. Translation: AAM61674.1.
PIRS52286.
RefSeqNP_196738.1. NM_121215.3.
UniGeneAt.23410.

3D structure databases

ProteinModelPortalQ42577.
SMRQ42577. Positions 68-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16327. 1 interaction.
IntActQ42577. 2 interactions.
STRING3702.AT5G11770.1-P.

Protein family/group databases

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

Proteomic databases

PaxDbQ42577.
PRIDEQ42577.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G11770.1; AT5G11770.1; AT5G11770.
GeneID831049.
KEGGath:AT5G11770.

Organism-specific databases

GeneFarm1829.
TAIRAT5G11770.

Phylogenomic databases

eggNOGCOG0377.
HOGENOMHOG000228249.
InParanoidQ42577.
KOK03940.
OMAQVRGVHS.
PhylomeDBQ42577.

Enzyme and pathway databases

BioCycARA:AT5G11770-MONOMER.
MetaCyc:AT5G11770-MONOMER.

Gene expression databases

GenevestigatorQ42577.

Family and domain databases

Gene3D3.40.50.700. 1 hit.
HAMAPMF_01356. NDH1_NuoB.
InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UQ_OxRdtase_20Kd_su.
[Graphical view]
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. nuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ42577.

Entry information

Entry nameNDUS7_ARATH
AccessionPrimary (citable) accession number: Q42577
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 121 of the entry and version 1 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