ID   NDUS7_NEUCR             Reviewed;         226 AA.
AC   O47950; Q7RZB4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 19.3 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-19.3kD;
DE            Short=CI-19.3kD;
DE   Flags: Precursor;
GN   ORFNames=G17A4.170, NCU03953;
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=10216160; DOI=10.1016/s0005-2728(99)00014-6;
RA   Sousa R., Barquera B., Duarte M., Finel M., Videira A.;
RT   "Characterisation of the last Fe-S cluster-binding subunit of Neurospora
RT   crassa complex I.";
RL   Biochim. Biophys. Acta 1411:142-146(1999).
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=[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 iron-sulfur (IP) fragment of the enzyme.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AJ001520; CAA04802.1; -; mRNA.
DR   EMBL; BX908812; CAF06152.1; -; Genomic_DNA.
DR   EMBL; CM002241; EAA28356.1; -; Genomic_DNA.
DR   RefSeq; XP_957592.1; XM_952499.3.
DR   AlphaFoldDB; O47950; -.
DR   SMR; O47950; -.
DR   STRING; 367110.O47950; -.
DR   TCDB; 3.D.1.6.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; 5141-EFNCRP00000003665; -.
DR   EnsemblFungi; EAA28356; EAA28356; NCU03953.
DR   GeneID; 3873682; -.
DR   KEGG; ncr:NCU03953; -.
DR   VEuPathDB; FungiDB:NCU03953; -.
DR   HOGENOM; CLU_055737_1_0_1; -.
DR   InParanoid; O47950; -.
DR   OMA; GCGGIEM; -.
DR   OrthoDB; 33762at2759; -.
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; IBA:GO_Central.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR   Gene3D; 3.40.50.12280; -; 1.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   NCBIfam; TIGR01957; nuoB_fam; 1.
DR   PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..226
FT                   /note="NADH-ubiquinone oxidoreductase 19.3 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000020032"
FT   REGION          40..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         166
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  24972 MW;  E48CB09C64AAAFC6 CRC64;
     MMSSVRTGAS MALRARPTAQ IVPFRAAAVA SISSSSRKDA TGAVAPAGAQ HGIARRERRE
     VPLPSQEGTK GAVQYALTTL DSIVNWARQS SLWPMTFGLA CCAVEMMHLS TPRYDQDRLG
     IIFRASPRQS DVMIVAGTLT NKMAPALRQV YDQMPDPRWV ISMGSCANGG GYYHYSYSVV
     RGCDRIVPVD IYVPGCPPTS EALMYGIFQL QRKMRNTKIT RMWYRK
//