NDUV2_ARATH
ID NDUV2_ARATH Reviewed; 255 AA.
AC O22769; Q940Z9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE Flags: Precursor;
GN OrderedLocusNames=At4g02580; ORFNames=T10P11.14;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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]
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This
CC is a component of the flavoprotein-sulfur (FP) 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 -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002330; AAC78260.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82198.1; -; Genomic_DNA.
DR EMBL; AY052326; AAK96519.1; -; mRNA.
DR EMBL; BT001140; AAN64531.1; -; mRNA.
DR PIR; T01091; T01091.
DR RefSeq; NP_567244.1; NM_116492.4.
DR PDB; 7A23; EM; 3.70 A; B=1-255.
DR PDB; 7A24; EM; 3.80 A; B=1-255.
DR PDB; 7AQR; EM; 2.91 A; E=1-255.
DR PDB; 7AR7; EM; 3.72 A; E=30-221.
DR PDB; 7AR8; EM; 3.53 A; E=1-255.
DR PDB; 7ARB; EM; 3.41 A; E=1-255.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; O22769; -.
DR SMR; O22769; -.
DR BioGRID; 13419; 1.
DR IntAct; O22769; 2.
DR STRING; 3702.AT4G02580.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; O22769; -.
DR PaxDb; O22769; -.
DR PRIDE; O22769; -.
DR ProteomicsDB; 251287; -.
DR EnsemblPlants; AT4G02580.1; AT4G02580.1; AT4G02580.
DR GeneID; 828130; -.
DR Gramene; AT4G02580.1; AT4G02580.1; AT4G02580.
DR KEGG; ath:AT4G02580; -.
DR Araport; AT4G02580; -.
DR TAIR; locus:2132387; AT4G02580.
DR eggNOG; KOG3196; Eukaryota.
DR HOGENOM; CLU_054362_1_1_1; -.
DR InParanoid; O22769; -.
DR OMA; VGKFHVQ; -.
DR OrthoDB; 1396088at2759; -.
DR PhylomeDB; O22769; -.
DR BioCyc; ARA:AT4G02580-MON; -.
DR BioCyc; MetaCyc:AT4G02580-MON; -.
DR PRO; PR:O22769; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22769; baseline and differential.
DR Genevisible; O22769; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..255
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT mitochondrial"
FT /id="PRO_0000020007"
FT REGION 214..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 171
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 175
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7ARB"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 255 AA; 28389 MW; BD61E8FEF47FE981 CRC64;
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI
LSYYPSNYKQ SAVIPLLDLA QQQNGGWLPV SAMNAVAKVI EVAPIRVYEV ATFYSMFNRA
KVGKYHLLVC GTTPCMIRGS RDIESALLDH LGVKRGEVTK DGLFSVGEME CMGCCVNAPM
ITVADYSNGS EGYTYNYFED VTPEKVVEIV EKLRKGEKPP HGTQNPKRIK CGPEGGNKTL
LGEPKPPQFR DLDAC
