ID   NDA1_SOLTU              Reviewed;         495 AA.
AC   Q9ST63;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Internal alternative NAD(P)H-ubiquinone oxidoreductase A1, mitochondrial;
DE            EC=1.6.5.9 {ECO:0000269|PubMed:10571867};
DE   AltName: Full=Internal alternative NADH dehydrogenase NDA1;
DE   AltName: Full=Internal non-phosphorylating NAD(P)H dehydrogenase 1;
DE            Short=StNDI1;
DE   AltName: Full=NADH:ubiquinone reductase (non-electrogenic) NDA1;
DE   Flags: Precursor;
GN   Name=NDA1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=10571867; DOI=10.1046/j.1365-313x.1999.00576.x;
RA   Rasmusson A.G., Svensson A.S., Knoop V., Grohmann L., Brennicke A.;
RT   "Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases
RT   in higher eukaryotes: two enzymes are present in potato mitochondria.";
RL   Plant J. 20:79-87(1999).
CC   -!- FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes
CC       the oxidation of mitochondrial NADH does not translocate protons across
CC       the inner mitochondrial membrane. {ECO:0000269|PubMed:10571867}.
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         Evidence={ECO:0000269|PubMed:10571867};
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         Evidence={ECO:0000269|PubMed:10571867};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:10571867}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10571867}; Matrix side
CC       {ECO:0000269|PubMed:10571867}. Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AJ245861; CAB52796.1; -; mRNA.
DR   RefSeq; NP_001305584.1; NM_001318655.1.
DR   AlphaFoldDB; Q9ST63; -.
DR   SMR; Q9ST63; -.
DR   PRIDE; Q9ST63; -.
DR   GeneID; 102598594; -.
DR   KEGG; sot:102598594; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q9ST63; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
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; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; NADP; Oxidoreductase; Peroxisome; Reference proteome; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..495
FT                   /note="Internal alternative NAD(P)H-ubiquinone
FT                   oxidoreductase A1, mitochondrial"
FT                   /id="PRO_0000422942"
FT   MOTIF           486..495
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  54902 MW;  6AFFC807BEB01340 CRC64;
     MPWFKNLIKI SKTITNQSSS YKSITPLASP LLTQFLQFTK QYSTNDHVVG LEATKSDQKP
     RIVVLGSGWA GCRLMKDIDT NIYDVVCVSP RNHMVFTPLL ASTCVGTLEF RSVAEPIGRI
     QPAVSTQPAS YFFLANCNAI DFDNHMIECE TVTEGVETLE AWKFNVSYDK LVIASGAHAL
     TFGIKGVNEH ATFLREVHHA QEIRRKLLLN LMLSDVPGVS EEEKRRLLHC VVVGGGPTGV
     EFSGELSDFI LKDVHQRYAH VKDYIHVTLI EANEILSSFD DRLRVYATNQ LTKSGVRLVR
     GLVQHVQPDN IILSDGTNVP YGLLVWSTGV GPSPFVNSLD IPKAKGRIGI DEWLRVPSVQ
     DVYSIGDCSG FLESTGRQVL PALAQVAERQ GKYLASLLNK VGKQGGGHAN CAQNINLGDP
     FVYKHLGSMA TIGRYKALVD LRESKEAKGV SLAGFTSFFV WRSAYLTRVV SWRNKIYVLI
     NWLTTLVFGR DISRI