ID   Q9UUU2_YARLL            Unreviewed;       488 AA.
AC   Q9UUU2; Q6CDX9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU364066};
GN   Name=nubm {ECO:0000313|EMBL:CAB65520.1};
GN   Synonyms=NUO51 {ECO:0000313|EMBL:AAF65194.2};
GN   ORFNames=YALI1_B26679g {ECO:0000313|EMBL:AOW01975.1};
OS   Yarrowia lipolytica (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=4952 {ECO:0000313|EMBL:CAB65520.1};
RN   [1] {ECO:0000313|EMBL:CAB65520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E 150 {ECO:0000313|EMBL:CAB65520.1};
RA   Kerscher S.J.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAB65520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E 150 {ECO:0000313|EMBL:CAB65520.1};
RX   PubMed=10924914; DOI=10.1016/S0005-2728(00)00154-7;
RA   Djafarzadeh Andabili R., Kerscher S., Zwicker K., Radermacher M.,
RA   Lindahl M., Schaegger H., Brandt U.;
RT   "Biophysical and structural characterization of proton-translocating NADH-
RT   dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia
RT   lipolytica.";
RL   Biochim. Biophys. Acta 1459:230-238(2000).
RN   [3] {ECO:0000313|EMBL:AAF65194.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11357863; DOI=10.1007/BF02817616;
RA   Rycovska A., Szabo R., Tomaska L., Nosek J.;
RT   "The respiratory complex I in yeast: isolation of a gene NUO51 coding for
RT   the nucleotide-binding subunit of NADH:ubiquinone oxidoreductase from the
RT   obligately aerobic yeast Yarrowia lipolytica.";
RL   Folia Microbiol. (Praha) 45:429-433(2000).
RN   [4] {ECO:0000313|EMBL:AOW01975.1, ECO:0000313|Proteomes:UP000182444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB89 {ECO:0000313|EMBL:AOW01975.1}, and CLIB89(W29)
RC   {ECO:0000313|Proteomes:UP000182444};
RX   PubMed=27603307;
RA   Magnan C., Yu J., Chang I., Jahn E., Kanomata Y., Wu J., Zeller M.,
RA   Oakes M., Baldi P., Sandmeyer S.;
RT   "Sequence Assembly of Yarrowia lipolytica Strain W29/CLIB89 Shows
RT   Transposable Element Diversity.";
RL   PLoS ONE 11:E0162363-E0162363(2016).
RN   [5] {ECO:0007829|PDB:6GCS}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.32 ANGSTROMS).
RX   PubMed=30277212; DOI=10.7554/elife.39213;
RA   Parey K., Brandt U., Xie H., Mills D.J., Siegmund K., Vonck J.,
RA   Kuhlbrandt W., Zickermann V.;
RT   "Cryo-EM structure of respiratory complex I at work. .";
RL   Elife 7:e39213-e39213(2018).
RN   [6] {ECO:0007829|PDB:6H8K}
RP   X-RAY CRYSTALLOGRAPHY (3.79 ANGSTROMS) OF 92-434 IN COMPLEX WITH [4FE-4S]
RP   CLUSTER.
RX   PubMed=30374105; DOI=10.1038/s41467-018-06955-y;
RA   Cabrera-Orefice A., Yoga E.G., Wirth C., Siegmund K., Zwicker K.,
RA   Guerrero-Castillo S., Zickermann V., Hunte C., Brandt U.;
RT   "Locking loop movement in the ubiquinone pocket of complex I disengages the
RT   proton pumps.";
RL   Nat. Commun. 9:4500-4500(2018).
RN   [7] {ECO:0007829|PDB:7B0N}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=33640456; DOI=10.1016/j.jbc.2021.100474;
RA   Hameedi M.A., Grba D.N., Richardson K.H., Jones A.J.Y., Song W.,
RA   Roessler M.M., Wright J.J., Hirst J.;
RT   "A conserved arginine residue is critical for stabilizing the N2 FeS
RT   cluster in mitochondrial complex I.";
RL   J. Biol. Chem. 296:100474-100474(2021).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000256|RuleBase:RU364066}.
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         Evidence={ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU364066}; Matrix side
CC       {ECO:0000256|RuleBase:RU364066}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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DR   EMBL; AF197536; AAF65194.2; -; Genomic_DNA.
DR   EMBL; CP017554; AOW01975.1; -; Genomic_DNA.
DR   EMBL; AJ249782; CAB65520.1; -; Genomic_DNA.
DR   PDB; 6GCS; EM; 4.32 A; B=1-488.
DR   PDB; 6H8K; X-ray; 3.79 A; B=92-434.
DR   PDB; 7B0N; EM; 3.70 A; F=1-488.
DR   PDBsum; 6GCS; -.
DR   PDBsum; 6H8K; -.
DR   VEuPathDB; FungiDB:YALI0_B20372g; -.
DR   VEuPathDB; FungiDB:YALI1_B26679g; -.
DR   eggNOG; KOG2658; Eukaryota.
DR   OMA; KWQFIPQ; -.
DR   Proteomes; UP000182444; Chromosome 1b.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   NCBIfam; TIGR01959; nuoF_fam; 1.
DR   PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6GCS, ECO:0007829|PDB:6H8K};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW   Electron transport {ECO:0000256|RuleBase:RU364066};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU364066};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW   Membrane {ECO:0000256|RuleBase:RU364066};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364066};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364066};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW   Oxidoreductase {ECO:0000313|EMBL:CAB65520.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU364066};
KW   Transit peptide {ECO:0000256|RuleBase:RU364066};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|RuleBase:RU364066}.
FT   DOMAIN          366..411
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
FT   BINDING         381
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0007829|PDB:6H8K"
FT   BINDING         384
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0007829|PDB:6H8K"
FT   BINDING         387
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0007829|PDB:6H8K"
FT   DISULFID        127..279
FT                   /evidence="ECO:0007829|PDB:7B0N"
SQ   SEQUENCE   488 AA;  53756 MW;  E4897C8832E23891 CRC64;
     MLRTTLHKRG LARLSRGFAT TQDATPKARQ YGGLKDQDRI FQNLYDNYGW DLASARKQGD
     WYKTKELILK GDTWIIDEIK KSGLRGRGGA GFPSGLKWSF MNPPGWEKNE GPRYLVVNAD
     EGEPGTCKDR EIMRKDPHKL VEGCLLAGRA MNATAAYIYI RGEFYNEAAV LQTAINEAYA
     AGLIGKDACG SGYDFDVYIH RGMGAYVCGE ETSLIESLEG KAGKPRLKPP FPAGVGLFGR
     PSTVTNVETV AVAPTILRRG GDWFASFGRE RNSGTKLFCI SGNVNEPCTV EEEMSIPLRE
     LLEKHCGGIK GGWDNLLGVI PGGCSVPILP KNICEDVLMD FDALKDVQSG LGTAAVIVIN
     KQQDVIRAIQ RFAAFYKHES CGQCTPCREG TTWLLKAMDR FRTGQAKERE IDMLYELTKD
     IEGHTICALG DAAAWPIQGL IRNFRPEMET RMKKFHDEVG AVSVGGWMKD ARVEKGKVVG
     APLPGVHH
//