INDA1_SOLTU
ID INDA1_SOLTU Reviewed; 495 AA.
AC M0ZYF3;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Internal alternative NAD(P)H-ubiquinone oxidoreductase A1, mitochondrial;
DE EC=1.6.5.9;
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; ORFNames=PGSC0003DMG400004168;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
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:0000250}.
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 -!- 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 -!- 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; Peripheral membrane
CC protein; Matrix side. Peroxisome.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEWC01009701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M0ZYF3; -.
DR SMR; M0ZYF3; -.
DR STRING; 4113.PGSC0003DMT400010678; -.
DR EnsemblPlants; PGSC0003DMT400010678; PGSC0003DMT400010678; PGSC0003DMG400004168.
DR EnsemblPlants; RHC06H1G0405.2.1; RHC06H1G0405.2.1; RHC06H1G0405.2.
DR Gramene; PGSC0003DMT400010678; PGSC0003DMT400010678; PGSC0003DMG400004168.
DR Gramene; RHC06H1G0405.2.1; RHC06H1G0405.2.1; RHC06H1G0405.2.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_3_1; -.
DR InParanoid; M0ZYF3; -.
DR OMA; FLANCNA; -.
DR OrthoDB; 1388419at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZYF3; baseline.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; ISS: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; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS: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 3: Inferred from homology;
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_0000422941"
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; 54911 MW; 5500CA342C749C03 CRC64;
MPWFKNLIKI SKTITNQSSS YKSITPLASP LLAQFLQFTK QYSTNDHVVG LEATKSDQKP
RIVVLGSGWA GCRLMKDIDT NIYDVVCVSP RNHMVFTPLL ASTCVGTLEF RSVAEPIGRI
QPAVSTQPAS YFFLANCNAI DFDNHMIQCQ TVTEGVETLE PWKFNVSYDK LVIASGAHAL
TFGIKGVNEH ATFLREVHHA QEIRRKLLLN LMLSDVPGVS EEEKRRLLHC VVVGGGPTGV
EFSGELSDFI LKDVHQRYAH VKDYIHVTLI EANEILSSFD DRLRVYATNQ LTKSGVRLVR
GLVQHVQPDK IILSDGTNVP YGLLVWSTGV GPSPFVNSLD IPKAKGRIGI DEWLRVPSVQ
DVYSIGDCSG FLESTGRQVL PALAQVAERQ GKYLASLLNK VGKEGGGHAN CAQNINLGDP
FVYKHLGSMA TIGRYKALVD LRESKEAKGV SLAGFTSFFV WRSAYLTRVV SWRNKIYVLI
NWLTTLVFGR DISRI
