NDUS2_CAFRO
ID NDUS2_CAFRO Reviewed; 398 AA.
AC Q9TAJ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 Cafeteria roenbergensis (Marine flagellate).
OG Mitochondrion.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Bicosoecida;
OC Cafeteriaceae; Cafeteria.
OX NCBI_TaxID=33653;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Burger G.;
RT "The mitochondrial genome of Cafeteria roenbergensis.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {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; AF193903; AAF05789.1; -; Genomic_DNA.
DR RefSeq; NP_051138.1; NC_000946.1.
DR AlphaFoldDB; Q9TAJ7; -.
DR SMR; Q9TAJ7; -.
DR GeneID; 800841; -.
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 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 PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 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..398
FT /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT /id="PRO_0000118588"
SQ SEQUENCE 398 AA; 45813 MW; 1BDDAF669C91404E CRC64;
MFIKRKLKET EIKDFTLNFG PQHPAAHGVL RLILELNGET IKNADPHIGL LHRGTEKLIE
NRNYLQALPY FDRLDYVSMM VQEHAYSLAV ERLYGINIPQ RAQWIRVLFS EITRILNHLL
AIGCHSMDVG AMTPLLWGFE EREKLMEFYE RVSGARMHAS YIRPGGVAQD LPSGFVEDVY
SFILDFSVRL DEIEELLTNN RIWKQRLVNV GIVTAKQAIQ NGFSGVLLRS TGIPWDLRRS
QPYEIYDKVP FRIPVGTRGD CYDRYLIRMQ EMRQSLRIMM ACLKYLPGGS IKSDDKKFVP
PLRWEMKNSM ESVIHHFKYF TEGFKVPAGQ TYAAVEAPKG EMGVFLISDG SNQPFRCKIK
APGFFHLQNL PEMTKHHMIA DVVTIIGTQD IVFGEVDR