NDUS2_PARTE
ID NDUS2_PARTE Reviewed; 400 AA.
AC P15689;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 7;
GN Name=NAD7;
OS Paramecium tetraurelia.
OG Mitochondrion.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock 51;
RX PubMed=2308823; DOI=10.1093/nar/18.1.173;
RA Pritchard A.E., Seilhamer J.J., Mahalingam R., Sable C.L., Venuti S.E.,
RA Cummings D.J.;
RT "Nucleotide sequence of the mitochondrial genome of Paramecium.";
RL Nucleic Acids Res. 18:173-180(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2670676; DOI=10.1016/0378-1119(89)90320-x;
RA Pritchard A.E., Venuti S.E., Ghalambor M.A., Sable C.L., Cummings D.J.;
RT "An unusual region of Paramecium mitochondrial DNA containing chloroplast-
RT like genes.";
RL Gene 78:121-134(1989).
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 (By
CC similarity). Component of the iron-sulfur (IP) fragment of the enzyme.
CC Component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000250}.
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.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X15917; CAA34042.1; -; Genomic_DNA.
DR EMBL; M26930; AAA79254.1; -; Genomic_DNA.
DR PIR; S07733; S07733.
DR AlphaFoldDB; P15689; -.
DR SMR; P15689; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; 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 Gene3D; 1.10.645.10; -; 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 PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Electron transport; Mitochondrion; NAD; Oxidoreductase; Respiratory chain;
KW Translocase; Transport; Ubiquinone.
FT CHAIN 1..400
FT /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT /id="PRO_0000118590"
SQ SEQUENCE 400 AA; 46077 MW; 1E66944DF516D4F7 CRC64;
MKAICVNFGP QHPAAHGVLR LILQLNGEVV EKMDIHIGLL HRGSEKLMET KPYLQSMPYF
DRLDYVSMMV QEHAYCLAIE ALLNTTNYTA NFVLVRTMFD ELTRILNHML AIACHALDIG
SMSSIFWAFE EREKIMEFYE RVCGRRMHAA FYRPNEVNLN FLSVKLLTDI LEFNNNCLTT
LSEMHNILTY NKIWKQRLVN IGSISYKDCL DFGLTGVMAR STGIKRDLRM DAFDTYANYY
YLNFRSYTGQ AGDSYDRFLI RMNEMSESIN IISQAIFKLT TSKNTCSPAS ILKALNKKKF
ISQTYKNEYS SMEKLITHFK YWSEGFKIQS NWTYQAVESP KGEFGVTLVS DGSNKPYRCK
VRSPAYHHLQ VLPKMSKGHL LADLSALIGT IDIVFGEIDR