ID   NDUS2_NEPOL             Reviewed;         398 AA.
AC   Q9TC96;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 7;
GN   Name=NAD7;
OS   Nephroselmis olivacea (Green alga).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10488238; DOI=10.2307/3871049;
RA   Turmel M., Lemieux C., Burger G., Lang B.F., Otis C., Plante I., Gray M.W.;
RT   "The complete mitochondrial DNA sequences of Nephroselmis olivacea and
RT   Pedinomonas minor: two radically different evolutionary patterns within the
RT   green algae.";
RL   Plant Cell 11:1717-1730(1999).
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). Component of the iron-sulfur (IP) fragment of the enzyme
CC       (By 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of about 45 different subunits. This is
CC       a component of the iron-sulfur (IP) fragment of the enzyme (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF110138; AAF03201.1; -; Genomic_DNA.
DR   RefSeq; YP_665674.1; NC_008239.1.
DR   AlphaFoldDB; Q9TC96; -.
DR   SMR; Q9TC96; -.
DR   GeneID; 4178038; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Respiratory chain; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..398
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   2"
FT                   /id="PRO_0000118584"
FT   BINDING         261
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         267
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         282
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   398 AA;  45476 MW;  BCBD8FE4AACB08EB CRC64;
     MAIEHASSIK KVKNFTLNFG PQHPAAHGVL RLVLELNGEV VARADPHIGL LHRGTEKLIE
     YKTYTQALPY FDRLDYVSMM CQEHAYSLAV EKLLHCEVPE RAQYIRVLFS EITRILNHLL
     ALTTHAMDVG ALTPFLWAFE EREKLIEFYE RVSGSRMHAA YIRPGGVACD LPANLCEDIY
     LFCQQFASRI DEMEEMLTNN RIWKQRLVDI GIVTAENAFA WGFSGVLLRG SGVAWDLRKT
     QPYDVYNRMI FDVPVGTQGD CYDRYLCRVE EMRQSIHIIM QCLNQLPKGM IKADDKKITP
     PSRSQMKQSM ESLIHHFKLF TEGYTVPNSE TYTSVEAPKG EFGVYLVSNG TNRPYRCKIR
     APGFLHLQGL DMMSKNHMLA DVVTIIGTQD IVFGEVDR