ID   NU2M_NEUCR              Reviewed;         583 AA.
AC   Q35140; M1RV23;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE            EC=7.1.1.2;
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=ndh-2; Synonyms=ND2; ORFNames=NCM007, NCU16006;
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].
RX   PubMed=3011426;
RA   de Vries H., Alzner-Deweerd B., Breitenberger C.A., Chang D.D.,
RA   de Jonge J.C., RajBhandary U.L.;
RT   "The E35 stopper mutant of Neurospora crassa: precise localization of
RT   deletion endpoints in mitochondrial DNA and evidence that the deleted DNA
RT   codes for a subunit of NADH dehydrogenase.";
RL   EMBO J. 5:779-785(1986).
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; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR   EMBL; X03793; CAA27418.1; -; Genomic_DNA.
DR   EMBL; KC683708; AGG15995.1; -; Genomic_DNA.
DR   PIR; A25096; A25096.
DR   RefSeq; YP_009126707.1; NC_026614.1.
DR   AlphaFoldDB; Q35140; -.
DR   SMR; Q35140; -.
DR   STRING; 367110.Q35140; -.
DR   TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   EnsemblFungi; AGG15995; AGG15995; NCU16006.
DR   GeneID; 23681559; -.
DR   KEGG; ncr:NCU16006; -.
DR   VEuPathDB; FungiDB:NCU16006; -.
DR   InParanoid; Q35140; -.
DR   Proteomes; UP000001805; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 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..583
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117612"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        174..176
FT                   /note="YIL -> HTS (in Ref. 1; CAA27418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="S -> F (in Ref. 1; CAA27418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="G -> R (in Ref. 1; CAA27418)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   583 AA;  65743 MW;  61908E24017C2F0B CRC64;
     MIIMTILSLL LSNAVTLRRD ISILFNRIVI IALIYCILHD TMSLSIISKG VGLHGGLLHI
     TNITQVFQIF IFLISILILQ LTSFDPIKKF YIMRHPRFIN KWPRAIGYSI PLSSIQAVLK
     DYLFKIQGFN KEHLKIIEYP LILLFVICGA VFLMSTNDLV SIFLSIELQS YGLYILSTIY
     RNSELSTTGG LIYFLLGGFS SCFILLGASL LYANSGTTSL DGLYIINSIS DVNDNMTSWY
     KSYYLNFSLL IFSVGFLFKV SAAPFHFWSP DVYDAIPTIV TTFVAIIAKI SIFILLLELV
     YHTNNYLSEF SWIYGLLVSS FLSLIIGTVV GLTQFRIKRL LAYSTISHLG FILLALSVST
     QSVESTQAFI FYLIQYSFSN LNVFIILITI GFSLYGYVWN NKEYKNLLDI NNSPVQLISQ
     LKGYFYLNPL LSLSLAITIF SFAGIPPLVG FFAKQMVLSA ALDNGYIFLS LIAILTSVVG
     AVYYLNIIKE IFFYSPGHKL KTVDVENTWP FPVKRDLKLN DSNAFSISYD RYTVSSPLSS
     GYTISSPFSI TISIITIVIL LFIFMNKEWL SMGTIMVQVL FST