ID NDH2_YARLI Reviewed; 582 AA.
AC F2Z699; O74931; Q6C0F6;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=External alternative NADH-ubiquinone oxidoreductase, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=External alternative NADH dehydrogenase;
DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic);
DE Flags: Precursor;
GN Name=NDH2; OrderedLocusNames=YALI0F25135g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=CLIB 122 / E 150;
RX PubMed=10381390; DOI=10.1242/jcs.112.14.2347;
RA Kerscher S.J., Okun J.G., Brandt U.;
RT "A single external enzyme confers alternative NADH:ubiquinone
RT oxidoreductase activity in Yarrowia lipolytica.";
RL J. Cell Sci. 112:2347-2354(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:10381390}.
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:10381390};
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:10381390};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for NADH {ECO:0000269|PubMed:10381390};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10381390}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10381390}; Intermembrane side
CC {ECO:0000269|PubMed:10381390}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ006852; CAA07265.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78667.1; -; Genomic_DNA.
DR RefSeq; XP_505856.1; XM_505856.1.
DR AlphaFoldDB; F2Z699; -.
DR SMR; F2Z699; -.
DR STRING; 284591.F2Z699; -.
DR EnsemblFungi; CAG78667; CAG78667; YALI0_F25135g.
DR GeneID; 2908423; -.
DR KEGG; yli:YALI0F25135g; -.
DR VEuPathDB; FungiDB:YALI0_F25135g; -.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; F2Z699; -.
DR OMA; QIPAQKD; -.
DR OrthoDB; 1434722at2759; -.
DR BRENDA; 1.6.5.9; 1122.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706:SF3; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 1: Evidence at protein level;
KW Coiled coil; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..582
FT /note="External alternative NADH-ubiquinone oxidoreductase,
FT mitochondrial"
FT /id="PRO_0000415492"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..501
FT /evidence="ECO:0000255"
FT COMPBIAS 48..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 277..313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 582 AA; 65815 MW; 2BD807DD0A026562 CRC64;
MLRLRPAVRA VSVARSVALT RSLHVSVAKF NKIEGTAPAG LPKEVKQTAG HQGHHQEIPK
PDENHPRRKK FHFWRSLWRL TYLSAIASLG YIGYRIYVIR NPSDQLPADP SKKTLVVLGS
GWGSVSFLKK LDTSNYNVIV VSPRNYFLFT PLLPSCPTGT IEHRSIMEPI RGIIRHKQAE
CQYLEADATK IDHEKRIVTI RSAVSENSKE EVIKEIPFDY LVVGVGAMSS TFGIPGVQEN
ACFLKEIPDA QQIRRTLMDC IEKAQFEKDP EVRKRLLHTV VVGGGPTGVE FAAELQDFFE
DDLRKWIPDI RDDFKVTLVE ALPNVLPSFS KKLIDYTEKT FSDEKISILT KTMVKSVDEN
VIRAEQTKGD GTKETLEMPY GTLVWATGNT VRPVVRELMS KIPAQKGSRR GLLVNEYLVV
EGTEGIWALG DCSATKYAPT AQVASQEGSY LANLLNGIAK TEDLNNEITN LEKQSEHTFD
EQERKNIFAQ LESKSRKLRR SRAMLPFEYS HQGSLAYIGS DRAVADLSFN FWGIMNWSSG
GTMTYYFWRS AYVSMCFSMR NKILVCIDWM KVRVFGRDIS RE
//
