ID   NDUS8_NEUCR             Reviewed;         219 AA.
AC   Q12644; Q7RV45; V5INI7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-23kD;
DE            Short=CI-23kD;
DE   Flags: Precursor;
GN   Name=nuo21.3c; ORFNames=NCU05009;
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].
RX   PubMed=8695631; DOI=10.1016/0005-2728(96)00033-3;
RA   Duarte M., Finel M., Videira A.;
RT   "Primary structure of a ferredoxin-like iron-sulfur subunit of complex I
RT   from Neurospora crassa.";
RL   Biochim. Biophys. Acta 1275:151-153(1996).
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=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. May
CC       donate electrons to 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X95547; CAA64794.1; -; mRNA.
DR   EMBL; CM002241; ESA42320.1; -; Genomic_DNA.
DR   EMBL; CM002241; ESA42321.1; -; Genomic_DNA.
DR   RefSeq; XP_011394933.1; XM_011396631.1.
DR   RefSeq; XP_011394934.1; XM_011396632.1.
DR   AlphaFoldDB; Q12644; -.
DR   SMR; Q12644; -.
DR   STRING; 367110.Q12644; -.
DR   TCDB; 3.D.1.6.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; 5141-EFNCRP00000001567; -.
DR   EnsemblFungi; ESA42320; ESA42320; NCU05009.
DR   EnsemblFungi; ESA42321; ESA42321; NCU05009.
DR   GeneID; 3872083; -.
DR   KEGG; ncr:NCU05009; -.
DR   VEuPathDB; FungiDB:NCU05009; -.
DR   HOGENOM; CLU_067218_0_1_1; -.
DR   InParanoid; Q12644; -.
DR   OrthoDB; 176717at2759; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR   Gene3D; 3.30.70.3270; -; 1.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   NCBIfam; TIGR01971; NuoI; 1.
DR   PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Repeat;
KW   Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..219
FT                   /note="NADH-ubiquinone oxidoreductase 23 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000020010"
FT   DOMAIN          111..140
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          150..179
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         120
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  24902 MW;  650E1CF3A7E61930 CRC64;
     MLTTTASSAA AVARQLTTRR VIAPSFVSQA IRTYATPAGP PPKGFRIPTP KTWDQEEEHV
     LDKNGRYFLL TEMFRGMYVA MEQFFRPPYT IYYPFEKGPI SPRFRGEHAL RRYPSGEERC
     IACKLCEAVC PAQAITIEAE ERADGSRRTT RYDIDMTKCI YCGFCQESCP VDAIVESPNA
     EYATETREEL LYNKEKLLSN GDKWEPELAA AIRADSPYR
//