ID   NDUS2_NICSY             Reviewed;         394 AA.
AC   Q36450;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 98.
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   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=7651330; DOI=10.1007/bf02456616;
RA   Pla M., Mathieu C., De Paepe R., Chetrit P., Vedel F.;
RT   "Deletion of the last two exons of the mitochondrial nad7 gene results in
RT   lack of the NAD7 polypeptide in a Nicotiana sylvestris CMS mutant.";
RL   Mol. Gen. Genet. 248:79-88(1995).
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       {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   -!- 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; X86706; CAA60392.1; -; mRNA.
DR   AlphaFoldDB; Q36450; -.
DR   SMR; Q36450; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; 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; 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.
PE   2: Evidence at transcript level;
KW   Electron transport; Mitochondrion; NAD; Oxidoreductase; Respiratory chain;
KW   Translocase; Transport; Ubiquinone.
FT   CHAIN           1..394
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   2"
FT                   /id="PRO_0000118585"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  44522 MW;  4DCA5173BAC46258 CRC64;
     MTTKNRQIKN FTSNFGPQHP AAHGVSRSVL EMNGEVVERA EPHIGLLQRG TEKLIEYKTY
     LQALPYSDRS EYVSMMAQEH AHSSAVERLL NCEVPLRAQY IRVLFREITR ISNHSLALTT
     HAMDVGASTP FLWAFEEREK LLEFYERVSG ARMHASFIRP GGVAQDLPLG LCIDIDSFTQ
     QFASRIDELE EMSTGNRIWK QRLVDIGTVT AQQAKDWGFS GVMLRGSGVC WDLRKAAPYD
     VHDQLDPDIP VGTRGDRYDR YCIRIEEMRQ SVRIIVQCLN QMPSGMIKAD DRKLCPPSRS
     RMKLSMESSI HHFEPYTEGF SVPAPSTYTA VEAPKGEFGV FLVSNGSNRP YRRKIRAPCF
     AHSQGLDSMS KHHMPADVVT IIGTQDIVSG EVDR