ID   NDUS2_NEUCR             Reviewed;         478 AA.
AC   P22142; Q7RVM8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-49kD;
DE            Short=CI-49kD;
DE   Flags: Precursor;
GN   Name=nuo-49; ORFNames=NCU02534;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-62.
RC   STRAIN=74-ORS-6a / FGSC 4200;
RX   PubMed=2147127; DOI=10.1007/bf00321116;
RA   Preis D., van der Pas J.C., Nehls U., Roehlen D.-A., Sackmann U.,
RA   Jahnke U., Weiss H.;
RT   "The 49 K subunit of NADH: ubiquinone reductase (complex I) from Neurospora
RT   crassa mitochondria: primary structure of the gene and the protein.";
RL   Curr. Genet. 18:59-64(1990).
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.
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;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Matrix side.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X54508; CAA38368.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA36429.2; -; Genomic_DNA.
DR   PIR; S13801; S13801.
DR   RefSeq; XP_965665.2; XM_960572.3.
DR   AlphaFoldDB; P22142; -.
DR   SMR; P22142; -.
DR   STRING; 367110.P22142; -.
DR   TCDB; 3.D.1.6.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; 5141-EFNCRP00000002181; -.
DR   EnsemblFungi; EAA36429; EAA36429; NCU02534.
DR   GeneID; 3881799; -.
DR   KEGG; ncr:NCU02534; -.
DR   VEuPathDB; FungiDB:NCU02534; -.
DR   HOGENOM; CLU_015134_1_1_1; -.
DR   InParanoid; P22142; -.
DR   OrthoDB; 191at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   NCBIfam; TIGR01962; NuoD; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW   Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2147127"
FT   CHAIN           43..478
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000019984"
FT   BINDING         341
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         347
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         362
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        417
FT                   /note="A -> G (in Ref. 1; CAA38368)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  54019 MW;  159C35BE3DF9D916 CRC64;
     MATTLFRLAG RNAKRHCMRQ STTIAHNLNS TRAFSASALR RYAEPSYEGQ GTRLVPTGDD
     FAPNNDLYGL EALKADGAPR VPPQDHILAR KVRHYTVNFG PQHPAAHGVL RLILELKGEE
     IVRADPHVGL LHRGTEKLCE YRTYLQALPY FDRLDYVSMM TNEQCFALAV EKLLNVEIPE
     RAKWIRTMFA EITRILNHLM SVLSHAMDVG ALTPFLWGFE EREKLMEFYE RVSGARLHAA
     YVRPGGVHQD IPLGLLDDIY MWATQFGDRI DETEEMLTDN RIWIDRLRGI GVVSAADALN
     LSFTGVMLRG SGVPWDIRKS QPYDAYDQVE FDVPVGINGD CYDRYLCRME EFRQSLRIIH
     QCLNKMPAGP VRVEDYKISP PPRSAMKENM EALIHHFLLY TKGYAVPPGD TYSAIEAPKG
     EMGVYVVSDG SERPYRVHIR APGFAHLGGF DHLSRGHMLA DAVAVIGTMD LVFGEVDR
//