ID NDUV1_ASPNG Reviewed; 496 AA. AC Q92406; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 117. DE RecName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial; DE EC=7.1.1.2; DE AltName: Full=Complex I-51kD; DE Short=CI-51kD; DE Flags: Precursor; GN Name=NUO51; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732; RX PubMed=8365409; DOI=10.1111/j.1432-1033.1993.tb18136.x; RA Proemper C., Schneider R., Weiss H.; RT "The role of the proton-pumping and alternative respiratory chain RT NADH:ubiquinone oxidoreductases in overflow catabolism of Aspergillus RT niger."; RL Eur. J. Biochem. 216:223-230(1993). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305}; CC Note=Binds 1 FMN. {ECO:0000305}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SUBUNIT: Complex I is composed of about 40 different subunits. This is CC a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane CC protein; Matrix side. CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family. CC {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; X64402; CAA45744.1; -; Genomic_DNA. DR AlphaFoldDB; Q92406; -. DR SMR; Q92406; -. DR PaxDb; 5061-CADANGAP00004183; -. DR VEuPathDB; FungiDB:An04g05640; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1126508; -. DR VEuPathDB; FungiDB:ATCC64974_80820; -. DR VEuPathDB; FungiDB:M747DRAFT_259879; -. DR eggNOG; KOG2658; Eukaryota. 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-KW. 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:InterPro. 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 3: Inferred from homology; KW 4Fe-4S; Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; KW Oxidoreductase; Respiratory chain; Transit peptide; Translocase; Transport; KW Ubiquinone. FT TRANSIT 1..30 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 31..496 FT /note="NADH-ubiquinone oxidoreductase 51 kDa subunit, FT mitochondrial" FT /id="PRO_0000019979" FT BINDING 98..107 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 214..261 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 396 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 399 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 439 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" SQ SEQUENCE 496 AA; 54452 MW; DE64F00A8E32B42A CRC64; MISRAAAPSS SIASLSSRSL RAQAPAARSF ATVQDNAPPV KHYGGLKDQD RIFTNLYGHH GADLKSAMKY GDWHRTKDIV LKGHDWLISE LKASGLRGRG GAGFPSGLKY SFMNFKDWDK DPRPRYLVVN ADEGEPGTCK DREIMRKDPQ KLIEGCLVVG RAMNANAAYM YIRGEFYQEA TVLQRAINEA YEAGLIGKNA CGTGYDFDVY IHRGMGAYVC GEETSLIESI EGKAGKPRLK PPFPAAVGLF GCPSTVTNVE TVAVTPTIMR RGASWFSSFG RERNAGTKLF CISGHVNNPC TVEEEMSISL RDVIDRHCGG VRGGWDNLLA VIPGGSSTPV LPKTICDDQL MDFDALKDSQ SGLGTAAVIV MDKSTDIVRA ISRLSTFYKH ESCGQCTPCR EGSKWTMHMM QRMEKGQARE REIDMLQELT KQVEGHTICA LGEAFAWPIQ GLIRHFRPEL EARIREYSKE VGGNGPYAGG WHPEARAEGK LISPGM //