NDUV1_ARATH
ID NDUV1_ARATH Reviewed; 486 AA.
AC Q9FNN5; Q8LAL7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE EC=7.1.1.2;
DE Flags: Precursor;
GN OrderedLocusNames=At5g08530; ORFNames=MAH20.9;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-30.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] 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 ECO:0000305|PubMed:25732537}; Peripheral membrane protein
CC {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AB006697; BAB10002.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91315.1; -; Genomic_DNA.
DR EMBL; AY092971; AAM12970.1; -; mRNA.
DR EMBL; BT006620; AAP31964.1; -; mRNA.
DR EMBL; AY087737; AAM65274.1; -; mRNA.
DR RefSeq; NP_196470.1; NM_120938.4.
DR PDB; 7A23; EM; 3.70 A; A=1-486.
DR PDB; 7A24; EM; 3.80 A; A=1-486.
DR PDB; 7AQR; EM; 2.91 A; F=1-486.
DR PDB; 7AR7; EM; 3.72 A; F=51-484.
DR PDB; 7AR8; EM; 3.53 A; F=1-486.
DR PDB; 7ARB; EM; 3.41 A; F=1-486.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9FNN5; -.
DR SMR; Q9FNN5; -.
DR BioGRID; 16030; 2.
DR IntAct; Q9FNN5; 2.
DR STRING; 3702.AT5G08530.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; Q9FNN5; -.
DR PaxDb; Q9FNN5; -.
DR PRIDE; Q9FNN5; -.
DR ProMEX; Q9FNN5; -.
DR ProteomicsDB; 239041; -.
DR EnsemblPlants; AT5G08530.1; AT5G08530.1; AT5G08530.
DR GeneID; 830752; -.
DR Gramene; AT5G08530.1; AT5G08530.1; AT5G08530.
DR KEGG; ath:AT5G08530; -.
DR Araport; AT5G08530; -.
DR TAIR; locus:2159522; AT5G08530.
DR eggNOG; KOG2658; Eukaryota.
DR HOGENOM; CLU_014881_1_0_1; -.
DR InParanoid; Q9FNN5; -.
DR OMA; CDDVIMD; -.
DR OrthoDB; 549172at2759; -.
DR PhylomeDB; Q9FNN5; -.
DR BioCyc; ARA:AT5G08530-MON; -.
DR BioCyc; MetaCyc:AT5G08530-MON; -.
DR PRO; PR:Q9FNN5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNN5; baseline and differential.
DR Genevisible; Q9FNN5; AT.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Electron transport; Flavoprotein; FMN; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 31..486
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 1,
FT mitochondrial"
FT /id="PRO_0000410789"
FT REGION 31..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..119
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250"
FT BINDING 222..270
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 405
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7ARB"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 337..347
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 386..400
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 406..423
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 450..481
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 486 AA; 53449 MW; DC751ADE75F7E9CE CRC64;
MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD
EDRIFTNLYG LHDPFLKGAM KRGDWHRTKD LVLKGTDWIV NEMKKSGLRG RGGAGFPSGL
KWSFMPKVSD GRPSYLVVNA DESEPGTCKD REIMRHDPHK LLEGCLIAGV GMRASAAYIY
IRGEYVNERL NLEKARREAY AAGLLGKNAC GSGYDFEVYI HFGAGAYICG EETALLESLE
GKQGKPRLKP PFPANAGLYG CPTTVTNVET VAVSPTILRR GPEWFSSFGR KNNAGTKLFC
ISGHVNKPCT VEEEMSIPLK ELIERHCGGV RGGWDNLLAI IPGGSSVPLI PKNICEDVLM
DFDALKAVQS GLGTAAVIVM DKSTDVVDAI ARLSYFYKHE SCGQCTPCRE GTGWLWMIME
RMKVGNAKLE EIDMLQEVTK QIEGHTICAL GDAAAWPVQG LIRHFRPELE RRIRERAERE
LLQAAA
