NDUV1_ASPNG
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 03-AUG-2022, entry version 112.
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}.
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DR EMBL; X64402; CAA45744.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92406; -.
DR SMR; Q92406; -.
DR STRING; 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; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 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 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; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 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
