ID   NDS8A_ARATH             Reviewed;         222 AA.
AC   Q42599; Q0WWI2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial;
DE            EC=7.1.1.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g79010; ORFNames=YUP8H12R.37, YUP8H12R_21;
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 [MRNA].
RC   STRAIN=cv. C24;
RX   PubMed=9037104; DOI=10.1007/s004380050342;
RA   Schmidt-Bleek K., Heiser V., Thieck O., Brennicke A., Grohmann L.;
RT   "The 28.5-kDa iron-sulfur protein of mitochondrial complex I is encoded in
RT   the nucleus in plants.";
RL   Mol. Gen. Genet. 253:448-454(1997).
RN   [2]
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   [3]
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   [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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
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). May donate electrons to ubiquinone. {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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of at least 49 different subunits. This
CC       is a component of the iron-sulfur (IP) fragment of the enzyme.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X84318; CAA59061.1; -; mRNA.
DR   EMBL; AC002986; AAC17054.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36193.1; -; Genomic_DNA.
DR   EMBL; AY048241; AAK82503.1; -; mRNA.
DR   EMBL; AY072622; AAL62013.1; -; mRNA.
DR   EMBL; AK226368; BAE98516.1; -; mRNA.
DR   EMBL; AY088308; AAM65847.1; -; mRNA.
DR   PIR; S52380; S52380.
DR   RefSeq; NP_178022.1; NM_106551.4.
DR   PDB; 7AQR; EM; 2.91 A; I=1-222.
DR   PDB; 7AR7; EM; 3.72 A; I=54-222.
DR   PDB; 7AR8; EM; 3.53 A; I=1-222.
DR   PDB; 7ARB; EM; 3.41 A; I=1-222.
DR   PDB; 8BED; EM; 2.03 A; I=1-222.
DR   PDB; 8BEE; EM; 2.04 A; I=1-222.
DR   PDB; 8BPX; EM; 2.09 A; I=1-222.
DR   PDB; 8BQ5; EM; 2.73 A; I=1-222.
DR   PDB; 8BQ6; EM; 2.80 A; I=1-222.
DR   PDBsum; 7AQR; -.
DR   PDBsum; 7AR7; -.
DR   PDBsum; 7AR8; -.
DR   PDBsum; 7ARB; -.
DR   PDBsum; 8BED; -.
DR   PDBsum; 8BEE; -.
DR   PDBsum; 8BPX; -.
DR   PDBsum; 8BQ5; -.
DR   PDBsum; 8BQ6; -.
DR   AlphaFoldDB; Q42599; -.
DR   EMDB; EMD-11873; -.
DR   EMDB; EMD-11875; -.
DR   EMDB; EMD-11876; -.
DR   EMDB; EMD-11878; -.
DR   EMDB; EMD-15998; -.
DR   EMDB; EMD-15999; -.
DR   EMDB; EMD-16168; -.
DR   EMDB; EMD-16171; -.
DR   EMDB; EMD-16172; -.
DR   SMR; Q42599; -.
DR   BioGRID; 29461; 29.
DR   IntAct; Q42599; 2.
DR   STRING; 3702.Q42599; -.
DR   SwissPalm; Q42599; -.
DR   PaxDb; 3702-AT1G79010-1; -.
DR   ProteomicsDB; 236819; -.
DR   EnsemblPlants; AT1G79010.1; AT1G79010.1; AT1G79010.
DR   GeneID; 844242; -.
DR   Gramene; AT1G79010.1; AT1G79010.1; AT1G79010.
DR   KEGG; ath:AT1G79010; -.
DR   Araport; AT1G79010; -.
DR   TAIR; AT1G79010; -.
DR   eggNOG; KOG3256; Eukaryota.
DR   HOGENOM; CLU_067218_5_0_1; -.
DR   InParanoid; Q42599; -.
DR   OMA; QFFRAPY; -.
DR   OrthoDB; 176717at2759; -.
DR   PhylomeDB; Q42599; -.
DR   BioCyc; ARA:AT1G79010-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G79010-MONOMER; -.
DR   PRO; PR:Q42599; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q42599; baseline and differential.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.3270; -; 1.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   NCBIfam; TIGR01971; NuoI; 1.
DR   PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   Genevisible; Q42599; AT.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Repeat;
KW   Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           ?..222
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   8-A, mitochondrial"
FT                   /id="PRO_0000020016"
FT   DOMAIN          114..143
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          153..182
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         123
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   HELIX           60..72
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   HELIX           197..218
FT                   /evidence="ECO:0007829|PDB:8BEE"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:8BEE"
SQ   SEQUENCE   222 AA;  25503 MW;  7C1F2264B0D0631B CRC64;
     MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW
     NTVFERSINT LFLTEMVRGL SLTLKYFFDP KVTINYPFEK GPLSPRFRGE HALRRYPTGE
     ERCIACKLCE AVCPAQAITI EAEEREDGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG
     PNFEFATETH EELLYDKEKL LENGDRWETE IAENLRSESL YR
//