NDH2_SCHPO
ID NDH2_SCHPO Reviewed; 551 AA.
AC O43090;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable NADH-ubiquinone oxidoreductase C947.15c, mitochondrial;
DE EC=1.6.5.9;
DE Flags: Precursor;
GN ORFNames=SPBC947.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the oxidation of NADH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17043.1; -; Genomic_DNA.
DR PIR; T40767; T40767.
DR RefSeq; NP_595261.1; NM_001021168.2.
DR AlphaFoldDB; O43090; -.
DR SMR; O43090; -.
DR BioGRID; 276744; 15.
DR STRING; 4896.SPBC947.15c.1; -.
DR iPTMnet; O43090; -.
DR MaxQB; O43090; -.
DR PaxDb; O43090; -.
DR PRIDE; O43090; -.
DR EnsemblFungi; SPBC947.15c.1; SPBC947.15c.1:pep; SPBC947.15c.
DR GeneID; 2540211; -.
DR KEGG; spo:SPBC947.15c; -.
DR PomBase; SPBC947.15c; -.
DR VEuPathDB; FungiDB:SPBC947.15c; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; O43090; -.
DR OMA; QSPVAMQ; -.
DR PhylomeDB; O43090; -.
DR PRO; PR:O43090; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISO:PomBase.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:PomBase.
DR GO; GO:0006116; P:NADH oxidation; ISS:PomBase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide; Ubiquinone.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..551
FT /note="Probable NADH-ubiquinone oxidoreductase C947.15c,
FT mitochondrial"
FT /id="PRO_0000337258"
FT BINDING 92..122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 255..291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 551 AA; 60781 MW; C8CE3C56F88108AC CRC64;
MSVSKARLQS VVRLSRTVPY SKTMVRSFHV SCAVKNSGNV PTPRNKSFFS RALEMAEVTS
SLSMLGAVAL FQSLRRLNNS SPKGKSGVPK KNIVVLGSGW GAVAAIKNLD PSLYNITLVS
PRDHFLFTPM LPSCTVGTLR LPSITEPIVA LFKGKIDPSN IHQAECTAID TSAKKVTIRG
TTEANEGKEA VIPYDTLVFA IGAGNQTFGI QGVRDHGCFL KEAGDAKKVF NRIFEILEQV
RFNKDLSPEE RARLLHITVV GGGPTGMEFA AEMQDFIDND VKDMFPELQK DIHVTLIEAA
PGVLPMFTKS LITYTENLFK NLNIKIMTKT VVKDVNEKNL IVQKTNPDGS KAMQEIPYGM
LVWAAGITAR PLTRTLMSSI PEQSGARKGL IVDEFFRVKG VPEMYAVGDC AFSGLPATAQ
VANQQGAWLA KNLNVEGKKF ALHERIQALE KQLGEKEAPS QVAGLKQQVE QLKLEPFKYH
HQGALAYVGD EKAIADLKLP FMKKMLPLQG IVGHTFWRLA YLNELISARS QFMVLIDWLK
TRLFGRYDAK V
