NDUS2_ARATH
ID NDUS2_ARATH Reviewed; 394 AA.
AC P93306;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 7;
GN Name=NAD7; OrderedLocusNames=AtMg00510;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07709).
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone (By
CC similarity). Component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This
CC is a component of the iron-sulfur (IP) fragment of the enzyme.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- RNA EDITING: Modified_positions=13 {ECO:0000269|PubMed:10611383}, 26
CC {ECO:0000269|PubMed:10611383}, 46 {ECO:0000269|PubMed:10611383}, 67
CC {ECO:0000269|PubMed:10611383}, 82 {ECO:0000269|PubMed:10611383}, 84
CC {ECO:0000269|PubMed:10611383}, 106 {ECO:0000269|PubMed:10611383}, 112
CC {ECO:0000269|PubMed:10611383}, 115 {ECO:0000269|PubMed:10611383}, 193
CC {ECO:0000269|PubMed:10611383}, 233 {ECO:0000269|PubMed:10611383}, 242
CC {ECO:0000269|PubMed:10611383}, 245 {ECO:0000269|PubMed:10611383}, 247
CC {ECO:0000269|PubMed:10611383}, 257 {ECO:0000269|PubMed:10611383}, 353
CC {ECO:0000269|PubMed:10611383}, 360 {ECO:0000269|PubMed:10611383}, 363
CC {ECO:0000269|PubMed:10611383}, 368 {ECO:0000269|PubMed:10611383}, 375
CC {ECO:0000269|PubMed:10611383};
CC -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC duplicated within the centromere of chromosome 2 resulting in the
CC duplication of the gene. The expression of the duplicated gene
CC (At2g07709) is not demonstrated. It is also probably not RNA edited and
CC therefore differs in all the positions known to be edited.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; Y08501; CAA69735.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_085511.1; NC_001284.2.
DR PDB; 7A23; EM; 3.70 A; G=1-394.
DR PDB; 7A24; EM; 3.80 A; G=1-394.
DR PDB; 7AR7; EM; 3.72 A; D=10-394.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AR7; -.
DR AlphaFoldDB; P93306; -.
DR SMR; P93306; -.
DR IntAct; P93306; 4.
DR STRING; 3702.ATMG00510.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR SwissPalm; P93306; -.
DR PeptideAtlas; P93306; -.
DR PRIDE; P93306; -.
DR Araport; ATMG00510; -.
DR eggNOG; KOG2870; Eukaryota.
DR InParanoid; P93306; -.
DR OrthoDB; 444312at2759; -.
DR BioCyc; ARA:ATMG00510-MON; -.
DR BioCyc; MetaCyc:ATMG00510-MON; -.
DR PRO; PR:P93306; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P93306; baseline and differential.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Respiratory chain; RNA editing; Translocase; Transport;
KW Ubiquinone.
FT CHAIN 1..394
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 2"
FT /id="PRO_0000118583"
SQ SEQUENCE 394 AA; 44962 MW; 6DE66B889FAA6BD0 CRC64;
MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY
LQALPYFDRS DYVSMMAQEH AYSLAVEKLL NCEVPLRAQY IRVLFCEITR ILNHLLALTT
HAMDVGALTP FLWAFEEREK LLEFYERVSG ARMHASFIRP GGVAQDLPLG LCRDIDSFTQ
QFASRIDELE EMLTGNRIWK QRLVDIGTVT AQQAKDWGFS GVMLRGPGVC WDLRRAAPYD
VYDQLDFDVP VGTRGDCYDR YCIRIEEMRQ SLRIIVQCLN QMPSGMIKAD DRKLCPPSRC
RMKLSMESSI HHFELYTEGF SVPASSTYTA VEAPKGEFGV FLVSNGSNRP YRCKIRAPGF
AHLQGLDFMS KHHMLADVVT IIGTQDIVFG EVDR
