NDA2_ARATH
ID NDA2_ARATH Reviewed; 508 AA.
AC O80874;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Internal alternative NAD(P)H-ubiquinone oxidoreductase A2, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=Internal alternative NADH dehydrogenase NDA2;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDA2;
DE Flags: Precursor;
GN Name=NDA2; OrderedLocusNames=At2g29990; ORFNames=F23F1;
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=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 [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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12972666; DOI=10.1104/pp.103.024208;
RA Michalecka A.M., Svensson A.S., Johansson F.I., Agius S.C., Johanson U.,
RA Brennicke A., Binder S., Rasmusson A.G.;
RT "Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases
RT have different evolutionary origin and show distinct responses to light.";
RL Plant Physiol. 133:642-652(2003).
RN [4]
RP REVIEW.
RX PubMed=15725055; DOI=10.1146/annurev.arplant.55.031903.141720;
RA Rasmusson A.G., Soole K.L., Elthon T.E.;
RT "Alternative NAD(P)H dehydrogenases of plant mitochondria.";
RL Annu. Rev. Plant Biol. 55:23-39(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16258072; DOI=10.1093/pcp/pci221;
RA Elhafez D., Murcha M.W., Clifton R., Soole K.L., Day D.A., Whelan J.;
RT "Characterization of mitochondrial alternative NAD(P)H dehydrogenases in
RT Arabidopsis: intraorganelle location and expression.";
RL Plant Cell Physiol. 47:43-54(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND MICROBODY TARGETING SIGNAL.
RX PubMed=18703057; DOI=10.1016/j.febslet.2008.07.061;
RA Carrie C., Murcha M.W., Kuehn K., Duncan O., Barthet M., Smith P.M.,
RA Eubel H., Meyer E., Day D.A., Millar A.H., Whelan J.;
RT "Type II NAD(P)H dehydrogenases are targeted to mitochondria and
RT chloroplasts or peroxisomes in Arabidopsis thaliana.";
RL FEBS Lett. 582:3073-3079(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=21841088; DOI=10.1104/pp.111.182352;
RA Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT "Defining the protein complex proteome of plant mitochondria.";
RL Plant Physiol. 157:587-598(2011).
RN [8]
RP INDUCTION BY AMMONIUM AND NITRATE.
RX PubMed=22732219; DOI=10.5483/bmbrep.2012.45.6.010;
RA Park B.S., Kim S.-I., Song J.T., Seo H.S.;
RT "Arabidopsis SIZ1 positively regulates alternative respiratory bypass
RT pathways.";
RL BMB Rep. 45:342-347(2012).
CC -!- FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes
CC the oxidation of mitochondrial NADH does not translocate protons across
CC the inner mitochondrial membrane. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Matrix side {ECO:0000269|PubMed:21841088}. Peroxisome.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, cotyledons, leaves,
CC stems, buds and flowers. {ECO:0000269|PubMed:12972666,
CC ECO:0000269|PubMed:16258072}.
CC -!- INDUCTION: Accumulates in response to ammonium but repressed by
CC nitrate. {ECO:0000269|PubMed:22732219}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AC004680; AAC31853.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08332.1; -; Genomic_DNA.
DR PIR; T02486; T02486.
DR RefSeq; NP_180560.1; NM_128553.3.
DR AlphaFoldDB; O80874; -.
DR SMR; O80874; -.
DR STRING; 3702.AT2G29990.1; -.
DR iPTMnet; O80874; -.
DR SwissPalm; O80874; -.
DR PaxDb; O80874; -.
DR PRIDE; O80874; -.
DR ProteomicsDB; 251318; -.
DR EnsemblPlants; AT2G29990.1; AT2G29990.1; AT2G29990.
DR GeneID; 817549; -.
DR Gramene; AT2G29990.1; AT2G29990.1; AT2G29990.
DR KEGG; ath:AT2G29990; -.
DR Araport; AT2G29990; -.
DR TAIR; locus:2045708; AT2G29990.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_3_1; -.
DR InParanoid; O80874; -.
DR OMA; WHLIDIA; -.
DR OrthoDB; 1388419at2759; -.
DR PhylomeDB; O80874; -.
DR BioCyc; ARA:AT2G29990-MON; -.
DR PRO; PR:O80874; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80874; baseline and differential.
DR Genevisible; O80874; AT.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; NADP; Oxidoreductase; Peroxisome; Reference proteome; Transit peptide;
KW Ubiquinone.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 47..508
FT /note="Internal alternative NAD(P)H-ubiquinone
FT oxidoreductase A2, mitochondrial"
FT /id="PRO_0000419504"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 499..508
FT /note="Microbody targeting signal"
FT BINDING 73..103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 240..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 56503 MW; 266A434E702A0C27 CRC64;
MFMIKNLTRI SPNTSSIITR FRNSGSSSLS YTLASRFCTA QETQIQSPAK IPNDVDRSQY
SGLPPTREGE KPRVVVLGSG WAGCRLMKGI DTNLYDVVCV SPRNHMVFTP LLASTCVGTL
EFRSVAEPIS RIQPAISREP GSFFFLANCS RLDADAHEVH CETLTDGLNT LKPWKFKIAY
DKLVIASGAE ASTFGIHGVM ENAIFLREVH HAQEIRRKLL LNLMLSDTPG ISKEEKRRLL
HCVVVGGGPT GVEFSGELSD FIMKDVRQRY AHVKDDIHVT LIEARDILSS FDDRLRRYAI
KQLNKSGVRF VRGIVKDVQS QKLILDDGTE VPYGLLVWST GVGPSPFVRS LGLPKDPTGR
IGIDEWMRVP SVQDVFAIGD CSGYLETTGK PTLPALAQVA EREGKYLANL LNAIGKGNGG
RANSAKEIEL GVPFVYKHLG SMATIGRYKA LVDLRESKDA KGISMTGFVS WFIWRSAYLT
RVISWRNRFY VAINWFTTFV FGRDISRI
