NDUS3_ARATH
ID NDUS3_ARATH Reviewed; 190 AA.
AC Q95748; A7KNI3; P93279;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 9;
GN Name=NAD9; OrderedLocusNames=AtMg00070;
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8776901; DOI=10.2307/3870308;
RA Sakamoto W., Kondo H., Murata M., Motoyoshi F.;
RT "Altered mitochondrial gene expression in a maternal distorted leaf mutant
RT of Arabidopsis induced by chloroplast mutator.";
RL Plant Cell 8:1377-1390(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-184, AND RNA EDITING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=17565941; DOI=10.1534/genetics.107.073585;
RA Bentolila S., Elliott L.E., Hanson M.R.;
RT "Genetic architecture of mitochondrial editing in Arabidopsis thaliana.";
RL Genetics 178:1693-1708(2008).
RN [5]
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). {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 inner membrane
CC {ECO:0000269|PubMed:14671022}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14671022}; Matrix side
CC {ECO:0000269|PubMed:14671022}.
CC -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 56 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 64 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 100 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 110 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 133 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 147 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941};
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; D82062; BAA11532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y08501; CAA69753.3; ALT_SEQ; Genomic_DNA.
DR EMBL; EF488926; ABS50638.1; -; mRNA.
DR EMBL; EF488927; ABS50639.1; -; mRNA.
DR RefSeq; NP_085479.1; NC_001284.2.
DR PDB; 7A23; EM; 3.70 A; F=1-190.
DR PDB; 7A24; EM; 3.80 A; F=1-190.
DR PDB; 7AQR; EM; 2.91 A; C=1-190.
DR PDB; 7AR7; EM; 3.72 A; C=1-185.
DR PDB; 7AR8; EM; 3.53 A; C=1-190.
DR PDB; 7ARB; EM; 3.41 A; C=1-190.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q95748; -.
DR SMR; Q95748; -.
DR BioGRID; 2; 8.
DR IntAct; Q95748; 4.
DR STRING; 3702.ATMG00070.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q95748; -.
DR PeptideAtlas; Q95748; -.
DR PRIDE; Q95748; -.
DR Araport; ATMG00070; -.
DR eggNOG; KOG1713; Eukaryota.
DR HOGENOM; CLU_042628_2_3_1; -.
DR InParanoid; Q95748; -.
DR OrthoDB; 1276923at2759; -.
DR BioCyc; ARA:ATMG00070-MON; -.
DR BioCyc; MetaCyc:ATMG00070-MON; -.
DR PRO; PR:Q95748; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; Q95748; baseline and differential.
DR Genevisible; Q95748; AT.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; RNA editing; Translocase; Transport; Ubiquinone.
FT CHAIN 1..190
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 3"
FT /id="PRO_0000118637"
FT CONFLICT 130
FT /note="R -> P (in Ref. 1; BAA11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="Q -> E (in Ref. 4; ABS50639/ABS50638)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 190 AA; 22880 MW; FCF70F540E71BC70 CRC64;
MDNQFIFKYS WETLPKKWVK KMERSEHGNR FDTNTDYLFQ LLCFLKLHTY TRVQVLIDIC
GVDYPSRKRR FEVVYNLLST RYNSRIRVQT SADEVTRISS VVSLFPSAGW WEREVWDMFG
VSFINHPDLR RILTDYGFEG HPLRKDFPLS GYVQVRYDDP EKRVVSEPIE MTQEFRYFDF
ASPWEQRSDG
