ID   NU5M_NEUCR              Reviewed;         715 AA.
AC   P05510; M1RM71;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 5;
GN   Name=ndh-5; Synonyms=ND5; ORFNames=NCM001, NCU16012;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=3035337; DOI=10.1007/bf00333589;
RA   Nelson M.A., Macino G.;
RT   "Structure and expression of the overlapping ND4L and ND5 genes of
RT   Neurospora crassa mitochondria.";
RL   Mol. Gen. Genet. 206:307-317(1987).
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).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA   Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.;
RT   "Mitochondrial genetics of Neurospora.";
RL   (In) Kueck U. (eds.);
RL   The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112,
RL   Springer-Verlag, Berlin-Heidelberg (2004).
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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; X05115; CAB37187.1; -; Genomic_DNA.
DR   EMBL; KC683708; AGG15999.1; -; Genomic_DNA.
DR   PIR; S10843; S10843.
DR   RefSeq; YP_009126711.1; NC_026614.1.
DR   AlphaFoldDB; P05510; -.
DR   SMR; P05510; -.
DR   STRING; 367110.P05510; -.
DR   TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   EnsemblFungi; AGG15999; AGG15999; NCU16012.
DR   GeneID; 23681563; -.
DR   KEGG; ncr:NCU16012; -.
DR   VEuPathDB; FungiDB:NCU16012; -.
DR   InParanoid; P05510; -.
DR   Proteomes; UP000001805; Mitochondrion.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..715
FT                   /note="NADH-ubiquinone oxidoreductase chain 5"
FT                   /id="PRO_0000118118"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        647..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        668..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   715 AA;  79817 MW;  CFAAF0F45FAAC277 CRC64;
     MYLSIIILPL LGSIVAGFFG RKVGVSGAQL ITCLSVIITT GLAILAFFEV GFNNIPVTIN
     LFRWIDSEWY NILWGFQFDS LTVAMLIPVL IISSLVHIYS ISYMSHDPHN QRFFSYLSLF
     TFMMIILVTA NNYLLMFVGW EGVGVCSYLL VSFWFTRIAA NQSSMSAFLT NRVGDCFLTI
     GMFVVLWTLG NLDYATVFSL APYINSDIAT IIGICLLIGA MAKSSQVGLH VWLPMAMEGP
     TPVSALIHAA TMVTAGVYLL MRSSPLIEYS STVLLLCLWL GAITTVFSSL IGLFQQDIKK
     VIAYSTMSQL GMMVIAIGLS SYNVALFHLI NHAFYKALLF LGAGSVIHAV ADNQDFRKFG
     GLKNYLPLTY SVMLIASLSL VAFPYMTGFY SKDFILESAY GQFSFSGVAV YIIATIGAIF
     TTLYSVKVLY LTFLANPNGY IHFYRHFILY ERLYVYVSYT GKEEFYLPKH MSKEINNLPR
     SVSGEGGFFL SLPLVILALF SIFFGFITKD IFIGLGSNFF IDNSLFIHPI HEIMIDTEFA
     VPTLFKLLPF IFTISFSLIA LVLSEKYPNL VVHFKLSRLG YNLFGFFNQR FLVELFYNKY
     ITNLVLDLGG QITKILDKGS IELLGPFGLE KVLIKWSKDI ASLSTSIVTN YALFILVGFI
     LYVFTFISLL EGGLDLNLSL FILLLSLTSS TSSSDSKEGK MIKKAVVSTK NKNIR