ID NDI1_YEAST Reviewed; 513 AA. AC P32340; D6W0G4; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial; DE EC=1.6.5.9; DE AltName: Full=Internal NADH dehydrogenase; DE AltName: Full=NADH:ubiquinone reductase (non-electrogenic); DE Flags: Precursor; GN Name=NDI1; OrderedLocusNames=YML120C; ORFNames=YM7056.06C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-36 AND 41-50. RC STRAIN=YP102; RX PubMed=1735444; DOI=10.1111/j.1432-1033.1992.tb16587.x; RA de Vries S., van Witzenburg R., Grivell L.A., Marres C.A.M.; RT "Primary structure and import pathway of the rotenone-insensitive NADH- RT ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae."; RL Eur. J. Biochem. 203:587-592(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=11502169; DOI=10.1021/bi010277r; RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., RA Schmitter J.-M.; RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular RT complex."; RL Biochemistry 40:9758-9769(2001). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200; RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; RT "Profiling phosphoproteins of yeast mitochondria reveals a role of RT phosphorylation in assembly of the ATP synthase."; RL Mol. Cell. Proteomics 6:1896-1906(2007). CC -!- FUNCTION: Catalyzes the oxidation of NADH generated inside the CC Mitochondrion. 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 -!- INTERACTION: CC P32340; P32340: NDI1; NbExp=5; IntAct=EBI-11961, EBI-11961; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:11502169}; Peripheral membrane protein CC {ECO:0000269|PubMed:11502169}; Matrix side CC {ECO:0000269|PubMed:11502169}. Note=Bound to the mitochondrial inner CC membrane facing the matrix site. CC -!- MISCELLANEOUS: Present with 5240 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; X61590; CAA43787.1; ALT_SEQ; Genomic_DNA. DR EMBL; Z49218; CAA89160.1; -; Genomic_DNA. DR EMBL; AY723851; AAU09768.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09778.1; -; Genomic_DNA. DR PIR; S26704; S26704. DR RefSeq; NP_013586.1; NM_001182483.1. DR PDB; 4G6G; X-ray; 2.39 A; A/B=24-513. DR PDB; 4G6H; X-ray; 2.26 A; A/B=24-513. DR PDB; 4G73; X-ray; 2.52 A; A/B=24-513. DR PDB; 4G74; X-ray; 2.48 A; A/B=24-513. DR PDB; 4G9K; X-ray; 2.70 A; A/B=43-513. DR PDB; 4GAP; X-ray; 2.90 A; A/B=43-513. DR PDB; 4GAV; X-ray; 3.00 A; A/B=43-513. DR PDB; 5YJW; X-ray; 1.85 A; A=30-513. DR PDB; 5YJX; X-ray; 3.21 A; A/B=28-513. DR PDBsum; 4G6G; -. DR PDBsum; 4G6H; -. DR PDBsum; 4G73; -. DR PDBsum; 4G74; -. DR PDBsum; 4G9K; -. DR PDBsum; 4GAP; -. DR PDBsum; 4GAV; -. DR PDBsum; 5YJW; -. DR PDBsum; 5YJX; -. DR AlphaFoldDB; P32340; -. DR SMR; P32340; -. DR BioGRID; 35084; 91. DR DIP; DIP-5554N; -. DR IntAct; P32340; 15. DR MINT; P32340; -. DR STRING; 4932.YML120C; -. DR iPTMnet; P32340; -. DR MaxQB; P32340; -. DR PaxDb; 4932-YML120C; -. DR PeptideAtlas; P32340; -. DR EnsemblFungi; YML120C_mRNA; YML120C; YML120C. DR GeneID; 854919; -. DR KEGG; sce:YML120C; -. DR AGR; SGD:S000004589; -. DR SGD; S000004589; NDI1. DR VEuPathDB; FungiDB:YML120C; -. DR eggNOG; KOG2495; Eukaryota. DR HOGENOM; CLU_021377_1_0_1; -. DR InParanoid; P32340; -. DR OMA; WIKLAFF; -. DR OrthoDB; 1434722at2759; -. DR BioCyc; MetaCyc:YML120C-MONOMER; -. DR BioCyc; YEAST:YML120C-MONOMER; -. DR BRENDA; 1.6.5.9; 984. DR BioGRID-ORCS; 854919; 1 hit in 10 CRISPR screens. DR PRO; PR:P32340; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P32340; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:SGD. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:SGD. DR GO; GO:0006116; P:NADH oxidation; IDA:SGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:SGD. 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; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR43706:SF10; ROTENONE-INSENSITIVE NADH-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2. DR UCD-2DPAGE; P32340; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Membrane; KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; KW Reference proteome; Transit peptide; Ubiquinone. FT TRANSIT 1..26 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:1735444" FT CHAIN 27..513 FT /note="Rotenone-insensitive NADH-ubiquinone oxidoreductase, FT mitochondrial" FT /id="PRO_0000021793" FT BINDING 55..85 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 229..265 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT VARIANT 10 FT /note="K -> R" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:5YJX" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:4G6H" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:4G6G" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:5YJW" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 77..84 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 91..96 FT /evidence="ECO:0007829|PDB:5YJW" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 111..115 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 122..133 FT /evidence="ECO:0007829|PDB:5YJW" FT TURN 134..137 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:4G6H" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:4G6G" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:4G6G" FT HELIX 198..215 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 223..228 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 238..253 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 260..265 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 283..295 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 311..319 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:4G74" FT STRAND 325..331 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 333..337 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:4G6G" FT HELIX 345..351 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 362..366 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:4G6H" FT STRAND 376..380 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 385..389 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 393..410 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 414..417 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:4G6H" FT HELIX 429..433 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 445..449 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 455..461 FT /evidence="ECO:0007829|PDB:5YJW" FT STRAND 464..471 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 472..485 FT /evidence="ECO:0007829|PDB:5YJW" FT HELIX 489..504 FT /evidence="ECO:0007829|PDB:5YJW" SQ SEQUENCE 513 AA; 57250 MW; E3A43D75A1ADCF3B CRC64; MLSKNLYSNK RLLTSTNTLV RFASTRSTGV ENSGAGPTSF KTMKVIDPQH SDKPNVLILG SGWGAISFLK HIDTKKYNVS IISPRSYFLF TPLLPSAPVG TVDEKSIIEP IVNFALKKKG NVTYYEAEAT SINPDRNTVT IKSLSAVSQL YQPENHLGLH QAEPAEIKYD YLISAVGAEP NTFGIPGVTD YGHFLKEIPN SLEIRRTFAA NLEKANLLPK GDPERRRLLS IVVVGGGPTG VEAAGELQDY VHQDLRKFLP ALAEEVQIHL VEALPIVLNM FEKKLSSYAQ SHLENTSIKV HLRTAVAKVE EKQLLAKTKH EDGKITEETI PYGTLIWATG NKARPVITDL FKKIPEQNSS KRGLAVNDFL QVKGSNNIFA IGDNAFAGLP PTAQVAHQEA EYLAKNFDKM AQIPNFQKNL SSRKDKIDLL FEENNFKPFK YNDLGALAYL GSERAIATIR SGKRTFYTGG GLMTFYLWRI LYLSMILSAR SRLKVFFDWI KLAFFKRDFF KGL //