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   24-JAN-2024, entry version 192.
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   PDB; 8BED; EM; 2.03 A; E=1-255.
DR   PDB; 8BPX; EM; 2.09 A; E=1-255.
DR   PDB; 8BQ5; EM; 2.73 A; E=1-255.
DR   PDB; 8BQ6; EM; 2.80 A; E=1-255.
DR   PDBsum; 7A23; -.
DR   PDBsum; 7A24; -.
DR   PDBsum; 7AQR; -.
DR   PDBsum; 7AR7; -.
DR   PDBsum; 7AR8; -.
DR   PDBsum; 7ARB; -.
DR   PDBsum; 8BED; -.
DR   PDBsum; 8BPX; -.
DR   PDBsum; 8BQ5; -.
DR   PDBsum; 8BQ6; -.
DR   AlphaFoldDB; O22769; -.
DR   EMDB; EMD-11873; -.
DR   EMDB; EMD-11875; -.
DR   EMDB; EMD-11876; -.
DR   EMDB; EMD-11878; -.
DR   EMDB; EMD-15998; -.
DR   EMDB; EMD-16168; -.
DR   EMDB; EMD-16171; -.
DR   EMDB; EMD-16172; -.
DR   SMR; O22769; -.
DR   BioGRID; 13419; 1.
DR   IntAct; O22769; 2.
DR   STRING; 3702.O22769; -.
DR   TCDB; 3.D.1.6.3; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   iPTMnet; O22769; -.
DR   PaxDb; 3702-AT4G02580-1; -.
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; AT4G02580; -.
DR   eggNOG; KOG3196; Eukaryota.
DR   HOGENOM; CLU_054362_1_1_1; -.
DR   InParanoid; O22769; -.
DR   OMA; IMSIYPE; -.
DR   OrthoDB; 177389at2759; -.
DR   PhylomeDB; O22769; -.
DR   BioCyc; ARA:AT4G02580-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G02580-MONOMER; -.
DR   PRO; PR:O22769; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O22769; baseline and differential.
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   CDD; cd03064; TRX_Fd_NuoE; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR042128; NuoE_dom.
DR   InterPro; IPR041921; NuoE_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01958; nuoE_fam; 1.
DR   PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
DR   Genevisible; O22769; AT.
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   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           90..100
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           133..136
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:7AQR"
FT   HELIX           144..151
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:7ARB"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   TURN            187..192
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:8BED"
FT   HELIX           203..215
FT                   /evidence="ECO:0007829|PDB:8BED"
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
//