NDA1_ARATH
ID NDA1_ARATH Reviewed; 510 AA.
AC Q8GWA1; Q8L5V3; Q9LML0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Internal alternative NAD(P)H-ubiquinone oxidoreductase A1, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=Internal alternative NADH dehydrogenase NDA1;
DE AltName: Full=Internal non-phosphorylating NAD(P)H dehydrogenase 1;
DE Short=AtNDI1;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDA1;
DE Flags: Precursor;
GN Name=NDA1; Synonyms=NDI1; OrderedLocusNames=At1g07180; ORFNames=F10K1.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, INDUCTION BY LIGHT, 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 [7]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=14630960; DOI=10.1104/pp.103.029363;
RA Moore C.S., Cook-Johnson R.J., Rudhe C., Whelan J., Day D.A., Wiskich J.T.,
RA Soole K.L.;
RT "Identification of AtNDI1, an internal non-phosphorylating NAD(P)H
RT dehydrogenase in Arabidopsis mitochondria.";
RL Plant Physiol. 133:1968-1978(2003).
RN [8]
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 [9]
RP INDUCTION BY LIGHT.
RX PubMed=15333756; DOI=10.1104/pp.104.046698;
RA Escobar M.A., Franklin K.A., Svensson A.S., Salter M.G., Whitelam G.C.,
RA Rasmusson A.G.;
RT "Light regulation of the Arabidopsis respiratory chain. Multiple discrete
RT photoreceptor responses contribute to induction of type II NAD(P)H
RT dehydrogenase genes.";
RL Plant Physiol. 136:2710-2721(2004).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
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 [11]
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).
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. Peroxisome.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, cotyledons, young leaves,
CC stems and flowers and, to a lower extent, in roots and buds.
CC {ECO:0000269|PubMed:12972666, ECO:0000269|PubMed:16258072}.
CC -!- INDUCTION: Follows a circadian regulation; up-regulated in a diurnal
CC manner. Up-regulated by high-light. {ECO:0000269|PubMed:12972666,
CC ECO:0000269|PubMed:15333756, ECO:0000269|PubMed:16258072}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:14630960}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC067971; AAF82202.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28089.1; -; Genomic_DNA.
DR EMBL; AK118982; BAC43558.1; -; mRNA.
DR EMBL; BT005564; AAO63984.1; -; mRNA.
DR EMBL; AY084663; AAM61225.1; -; mRNA.
DR PIR; H86206; H86206.
DR RefSeq; NP_563783.1; NM_100592.5.
DR AlphaFoldDB; Q8GWA1; -.
DR SMR; Q8GWA1; -.
DR STRING; 3702.AT1G07180.1; -.
DR iPTMnet; Q8GWA1; -.
DR PaxDb; Q8GWA1; -.
DR PRIDE; Q8GWA1; -.
DR ProteomicsDB; 236814; -.
DR EnsemblPlants; AT1G07180.1; AT1G07180.1; AT1G07180.
DR GeneID; 837229; -.
DR Gramene; AT1G07180.1; AT1G07180.1; AT1G07180.
DR KEGG; ath:AT1G07180; -.
DR Araport; AT1G07180; -.
DR TAIR; locus:2007427; AT1G07180.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_3_1; -.
DR InParanoid; Q8GWA1; -.
DR OMA; DHCIFLD; -.
DR OrthoDB; 1388419at2759; -.
DR PhylomeDB; Q8GWA1; -.
DR BioCyc; ARA:AT1G07180-MON; -.
DR PRO; PR:Q8GWA1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GWA1; baseline and differential.
DR Genevisible; Q8GWA1; 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:0003954; F:NADH dehydrogenase activity; IMP:TAIR.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP: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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; NADP; Oxidoreductase; Peroxisome; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..510
FT /note="Internal alternative NAD(P)H-ubiquinone
FT oxidoreductase A1, mitochondrial"
FT /id="PRO_0000419503"
FT MOTIF 501..510
FT /note="Microbody targeting signal"
FT BINDING 75..105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 242..278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 337
FT /note="P -> L (in Ref. 5; AAM61225)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="A -> T (in Ref. 5; AAM61225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56628 MW; 12BA0AB1A72AE6AB CRC64;
MLWIKNLARI SQTTSSSVGN VFRNPESYTL SSRFCTALQK QQVTDTVQAK EDVVNALEPQ
RYDGLAPTKE GEKPRVLVLG SGWAGCRVLK GIDTSIYDVV CVSPRNHMVF TPLLASTCVG
TLEFRSVAEP ISRIQPAISR EPGSYYFLAN CSKLDADNHE VHCETVTEGS STLKPWKFKI
AYDKLVLACG AEASTFGING VLENAIFLRE VHHAQEIRRK LLLNLMLSEV PGIGEDEKKR
LLHCVVVGGG PTGVEFSGEL SDFIMKDVRQ RYSHVKDDIR VTLIEARDIL SSFDDRLRHY
AIKQLNKSGV KLVRGIVKEV KPQKLILDDG TEVPYGPLVW STGVGPSSFV RSLDFPKDPG
GRIGIDEWMR VPSVQDVFAI GDCSGYLEST GKSTLPALAQ VAEREGKYLA NLFNVMGKAG
GGRANSAKEM ELGEPFVYKH LGSMATIGRY KALVDLRESK EGKGISMAGF LSWFIWRSAY
LTRVVSWRNR FYVAINWLTT FVFGRDISRI
