NDUS1_ARATH
ID NDUS1_ARATH Reviewed; 748 AA.
AC Q9FGI6; Q940B1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1467;
DE Flags: Precursor;
GN Name=EMB1467; OrderedLocusNames=At5g37510; ORFNames=MPA22.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:BAB10668.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 511-523.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
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). This is the largest subunit of complex I and it is a
CC component of the iron-sulfur (IP) fragment of the enzyme. It may form
CC part of the active site crevice where NADH is oxidized (By similarity).
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
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 {ECO:0000250}.
CC Note=Matrix and cytoplasmic side of the mitochondrial inner membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FGI6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025630; BAB10668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94200.1; -; Genomic_DNA.
DR EMBL; AY056140; AAL07219.1; -; mRNA.
DR RefSeq; NP_568550.1; NM_123110.2. [Q9FGI6-1]
DR RefSeq; NP_851103.1; NM_180772.2.
DR PDB; 7A23; EM; 3.70 A; C=1-748.
DR PDB; 7A24; EM; 3.80 A; C=1-748.
DR PDB; 7AQR; EM; 2.91 A; G=1-748.
DR PDB; 7AR7; EM; 3.72 A; G=57-744.
DR PDB; 7AR8; EM; 3.53 A; G=1-748.
DR PDB; 7ARB; EM; 3.41 A; G=1-748.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9FGI6; -.
DR SMR; Q9FGI6; -.
DR BioGRID; 18980; 3.
DR IntAct; Q9FGI6; 2.
DR STRING; 3702.AT5G37510.2; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q9FGI6; -.
DR MetOSite; Q9FGI6; -.
DR PaxDb; Q9FGI6; -.
DR PRIDE; Q9FGI6; -.
DR ProteomicsDB; 251103; -. [Q9FGI6-1]
DR EnsemblPlants; AT5G37510.2; AT5G37510.2; AT5G37510. [Q9FGI6-1]
DR GeneID; 833729; -.
DR Gramene; AT5G37510.2; AT5G37510.2; AT5G37510. [Q9FGI6-1]
DR KEGG; ath:AT5G37510; -.
DR Araport; AT5G37510; -.
DR TAIR; locus:2169871; AT5G37510.
DR eggNOG; KOG2282; Eukaryota.
DR InParanoid; Q9FGI6; -.
DR OrthoDB; 1095510at2759; -.
DR PhylomeDB; Q9FGI6; -.
DR BioCyc; ARA:AT5G37510-MON; -.
DR BioCyc; MetaCyc:AT5G37510-MON; -.
DR PRO; PR:Q9FGI6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGI6; baseline and differential.
DR Genevisible; Q9FGI6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR CDD; cd00207; fer2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NuoG_C.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 4Fe-4S; Alternative splicing;
KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..748
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 1, mitochondrial"
FT /id="PRO_0000019972"
FT DOMAIN 72..150
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 150..189
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 287..343
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 170
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 302..317
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 321..326
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 432..436
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 452..465
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 489..497
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 501..507
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 526..539
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 673..681
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:7ARB"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 727..730
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 734..741
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 748 AA; 81525 MW; C83400F148E73F44 CRC64;
MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV
GGARVHFSNP EDAIEVFVDG YAVKVPKGFT VLQACEVAGV DIPRFCYHSR LSIAGNCRMC
LVEVEKSPKP VASCAMPALP GMKIKTDTPI AKKAREGVME FLLMNHPLDC PICDQGGECD
LQDQSMAFGS DRGRFTEMKR SVVDKNLGPL VKTVMTRCIQ CTRCVRFASE VAGVQDLGIL
GRGSGEEIGT YVEKLMTSEL SGNVIDICPV GALTSKPFAF KARNWELKAT ETIDVSDAVG
SNIRVDSRGP EVMRIIPRLN EDINEEWISD KTRFCYDGLK RQRLSDPMIR DSDGRFKAVS
WRDALAVVGD IIHQVKPDEI VGVAGQLSDA ESMMVLKDFV NRMGSDNVWC EGTAAGVDAD
LRYSYLMNTS ISGLENADLF LLIGTQPRVE AAMVNARICK TVRASNAKVG YVGPPAEFNY
DCKHLGTGPD TLKEIAEGRH PFCTALKNAK NPAIIVGAGL FNRTDKNAIL SSVESIAQAN
NVVRPDWNGL NFLLQYAAQA AALDLGLIQQ SAKALESAKF VYLMGADDVN VDKIPKDAFV
VYQGHHGDKA VYRANVILPA SAFTEKEGTY ENTEGFTQQT VPAVPTVGDA RDDWKIVRAL
SEVSGVKLPY NSIEGVRSRI KSVAPNLVHT DEREPAAFGP SLKPECKEAM STTPFQTVVE
NFYMTNSITR ASKIMAQCSA VLLKKPFV
