NDUV1_NEUCR
ID NDUV1_NEUCR Reviewed; 493 AA.
AC P24917; Q7RV82;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
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=nuo-51; ORFNames=B10H18.210, NCU04044;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=1832016; DOI=10.1016/0167-4781(91)90049-r;
RA Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.-A.,
RA van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H.;
RT "Primary structures of two subunits of NADH: ubiquinone reductase from
RT Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble
RT NAD-reducing hydrogenase of Alcaligenes eutrophus.";
RL Biochim. Biophys. Acta 1090:133-138(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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.
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.
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; X56227; CAA39676.1; -; mRNA.
DR EMBL; BX897678; CAE85605.1; -; Genomic_DNA.
DR EMBL; CM002241; EAA28423.1; -; Genomic_DNA.
DR PIR; S17663; S17663.
DR RefSeq; XP_957659.1; XM_952566.2.
DR AlphaFoldDB; P24917; -.
DR SMR; P24917; -.
DR STRING; 5141.EFNCRP00000003696; -.
DR TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PRIDE; P24917; -.
DR EnsemblFungi; EAA28423; EAA28423; NCU04044.
DR GeneID; 3873830; -.
DR KEGG; ncr:NCU04044; -.
DR VEuPathDB; FungiDB:NCU04044; -.
DR HOGENOM; CLU_014881_1_0_1; -.
DR InParanoid; P24917; -.
DR OMA; CDDVIMD; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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 2: Evidence at transcript level;
KW 4Fe-4S; Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT CHAIN 28..493
FT /note="NADH-ubiquinone oxidoreductase 51 kDa subunit,
FT mitochondrial"
FT /id="PRO_0000019980"
FT BINDING 96..105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 212..259
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 397
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 437
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT CONFLICT 260..261
FT /note="VA -> AV (in Ref. 1; CAA39676)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="A -> R (in Ref. 1; CAA39676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54241 MW; 351B01F00602B06E CRC64;
MLSRTAAPTK ASARTLSRAA AEQCRTFATV QDGSANPVRH YGGLKDQDRI FQNLYGRYPP
DLKHAKKMGD WHKTKEILLK GHDWIIGEVK ASGLRGRGGA GFPSGLKWSF MNFKDWDKDD
KPRYLVVNAD EGEPGTCKDR EIMRKDPHKL VEGCLVAGRA MNATAAYIYI RGEFIQEAAI
LQNAINEAYA DGLIGKNACG SGYDFDVYLH RGAGAYVCGE ETSLIESLEG KPGKPRLKPP
FPAAVGLFGC PSTVANVETV AVAPTICRRG GNWFAGFGRE RNQGTKLFCI SGHVNNPCTV
EEEMSIPMRE LIDKHCGGVR GGWDNLLAVI PGGSSTPILP KHICDTQLMD FDALKDSQSG
LGTAALIVMD KSTDVVRAIS RLSHFYRHES CGQCTPCREG SKWTEQIMKR FEKGQGRERE
IDMLQELTKQ VEGHTICALG EAFAWPIQGL IRHFRPELEA RIRKFAQENG GEALAGGWQR
NARQQGKLVS PGM
