NDB4_ARATH
ID NDB4_ARATH Reviewed; 582 AA.
AC Q9SKT7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=External alternative NAD(P)H-ubiquinone oxidoreductase B4, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=External alternative NADH dehydrogenase NDB4;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDB4;
DE Flags: Precursor;
GN Name=NDB4; OrderedLocusNames=At2g20800; ORFNames=F5H14;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 [5]
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 [6]
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).
RN [7]
RP INDUCTION BY ABIOTIC STRESSES.
RX PubMed=16027974; DOI=10.1007/s11103-005-5514-7;
RA Clifton R., Lister R., Parker K.L., Sappl P.G., Elhafez D., Millar A.H.,
RA Day D.A., Whelan J.;
RT "Stress-induced co-expression of alternative respiratory chain components
RT in Arabidopsis thaliana.";
RL Plant Mol. Biol. 58:193-212(2005).
RN [8]
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 [9]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17673460; DOI=10.1074/jbc.m704674200;
RA Geisler D.A., Broselid C., Hederstedt L., Rasmusson A.G.;
RT "Ca2+-binding and Ca2+-independent respiratory NADH and NADPH
RT dehydrogenases of Arabidopsis thaliana.";
RL J. Biol. Chem. 282:28455-28464(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21659327; DOI=10.1093/pcp/pcr073;
RA Smith C., Barthet M., Melino V., Smith P., Day D., Soole K.;
RT "Alterations in the mitochondrial alternative NAD(P)H Dehydrogenase NDB4
RT lead to changes in mitochondrial electron transport chain composition,
RT plant growth and response to oxidative stress.";
RL Plant Cell Physiol. 52:1222-1237(2011).
RN [11]
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).
CC -!- FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes
CC the oxidation of mitochondrial NADH does not translocate protons across
CC the inner mitochondrial membrane (By similarity). NAD(P)H
CC dehydrogenase; more efficient on NADH. {ECO:0000250,
CC ECO:0000269|PubMed:17673460, ECO:0000269|PubMed:21659327}.
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 -!- ACTIVITY REGULATION: No effect of calcium ions on activity.
CC {ECO:0000269|PubMed:17673460}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8 with NADPH as substrate and 6.8-7.8 with NADH as
CC substrate. {ECO:0000269|PubMed:17673460};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side {ECO:0000269|PubMed:21841088}. Peroxisome
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, cotyledons, stems,
CC buds and flowers and, to a lower extent, in stems and leaves.
CC {ECO:0000269|PubMed:12972666, ECO:0000269|PubMed:16258072}.
CC -!- INDUCTION: Induced by chloramphenicol (Chl), erythromycin (Ery),
CC paraquat (Par), rotenone (Rot) and salicylic acid (SA).
CC {ECO:0000269|PubMed:16027974}.
CC -!- DISRUPTION PHENOTYPE: Lower reactive oxygen species formation and
CC altered phenotype (e.g. growth rate, root:shoot ratios and leaf area).
CC Lower leaf area early in development followed by a prompt subsequent
CC increase in leaf area leading to larger leaves in mature plants. Better
CC tolerance to salinity stress. These phenotypes are probably due to an
CC enhanced expression of NDB2 and AOX. {ECO:0000269|PubMed:21659327}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AC006234; AAD20915.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07074.1; -; Genomic_DNA.
DR EMBL; DQ446535; ABE65838.1; -; mRNA.
DR PIR; E84593; E84593.
DR RefSeq; NP_179673.1; NM_127645.4.
DR AlphaFoldDB; Q9SKT7; -.
DR SMR; Q9SKT7; -.
DR BioGRID; 1962; 2.
DR IntAct; Q9SKT7; 1.
DR STRING; 3702.AT2G20800.1; -.
DR SwissPalm; Q9SKT7; -.
DR PaxDb; Q9SKT7; -.
DR PRIDE; Q9SKT7; -.
DR ProteomicsDB; 251097; -.
DR EnsemblPlants; AT2G20800.1; AT2G20800.1; AT2G20800.
DR GeneID; 816609; -.
DR Gramene; AT2G20800.1; AT2G20800.1; AT2G20800.
DR KEGG; ath:AT2G20800; -.
DR Araport; AT2G20800; -.
DR TAIR; locus:2051431; AT2G20800.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; Q9SKT7; -.
DR OMA; EYKEAEC; -.
DR OrthoDB; 487337at2759; -.
DR PhylomeDB; Q9SKT7; -.
DR BioCyc; ARA:AT2G20800-MON; -.
DR PRO; PR:Q9SKT7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKT7; baseline and differential.
DR Genevisible; Q9SKT7; AT.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome; Transit peptide; Ubiquinone.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..582
FT /note="External alternative NAD(P)H-ubiquinone
FT oxidoreductase B4, mitochondrial"
FT /id="PRO_0000419508"
FT DOMAIN 384..419
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 573..582
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT BINDING 65..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 227..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65372 MW; C8412C4A30299720 CRC64;
MSFHSFYQRA SSLFKAYPST SKILLLSTFS GGGGVLVYSD SNPLKRILHA DATLDSDGNP
IRKKKVVVLG SGWSGYSFLS YLNNPNYDVQ VVSPRNFFLF TPLLPSVTNG TVEARSIVEP
IRGLMRKKGF EYKEAECVKI DASNKKIHCR SKEGSSLKGT TEFDMDYDIL ILAVGAKPNT
FNTPGVEEHA YFLKEAEDAL NIRHSVIDCF ERASLPNLTE EERKKILHFV VVGGGPTGVE
FSAELHDFLV QDVAKIYPKV QEFTKITLLE AGDHILNMFD KRITAFAEEK FQRDGIDLKT
GSMVVGVTAD EISTKERETG KIVSEPYGMV VWSTGIGSRP VIKDFMQQIG QGQRRVLATD
EWLRVEGCDG VYALGDTATI NQRRVMEDIA AIFNKADKGN TGTLKKKDFN SVVKDICQRY
PQVELYLKKN KLKNIANLLK SANGEDTQVN IEKFKQALSE VDSQMKNLPA TAQVASQQGK
YLAKCFNKME KCEKKPEGPL RFRGEGRHRF QPFRYRHFGS FAPLGGEQTA AELPGDWVSI
GHSSQWLWYS VYASKLVSWR TRMLVISDWT RRFVFGRDSS SI
