ID   NDUS2_DICCI             Reviewed;         406 AA.
AC   Q2LCR5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
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; Synonyms=ndufs2;
OS   Dictyostelium citrinum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=361072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18413355; DOI=10.1093/molbev/msn088;
RA   Heidel A.J., Gloeckner G.;
RT   "Mitochondrial genome evolution in the social amoebae.";
RL   Mol. Biol. Evol. 25:1440-1450(2008).
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       {ECO:0000250|UniProtKB:O75306}.
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   -!- SUBUNIT: Complex I is composed of 45 different subunits. Component of
CC       the iron-sulfur (IP) fragment of the enzyme.
CC       {ECO:0000250|UniProtKB:O75306}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O75306}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O75306}; Matrix side
CC       {ECO:0000250|UniProtKB:O75306}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; DQ336395; ABC60378.1; -; Genomic_DNA.
DR   RefSeq; YP_492627.1; NC_007787.2.
DR   AlphaFoldDB; Q2LCR5; -.
DR   SMR; Q2LCR5; -.
DR   GeneID; 3912609; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; 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; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Oxidoreductase; Respiratory chain; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..406
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT                   /id="PRO_0000312396"
SQ   SEQUENCE   406 AA;  46817 MW;  5811AF68D71F86BA CRC64;
     MLNISKIFEE VKVMKNFTLN FGPQHPAAHG VLRLIVELES ENVVRVEPHI GLLHRGTEKL
     IEGKTYTQAL PYFDRLDYVS MNVQEHAYSL AVERLYLDSL DIELEIPQRA KVIRVLFSEI
     TRVLNHIMAT TTHAMDVGAL TPFLWAFEER EKLMEFYERV SGARMHAAYI RPGGVAFDLP
     MNISEDIYKF VIQYRKRLEE IEDMLINNRI WKQRLVDIGI VSAEEALNYG FTGPLLRGAG
     IVYDIRKNYP YDDYDKYDFK IIIGEENNSY TRFIIRMKEM YQSLAIIEQA LNNLRPGLIK
     LEGVNITAPD RAFVKKDMES CINHFKFFSE GFIIPANENY TIVEAPKGEF GIYLNANDTA
     KPYRCRIKAP GFLHLQGLNM MSKDHLLADV VTLIGTQDIV FGEVDR