ID   NDUS2_DICDI             Reviewed;         406 AA.
AC   Q23883; Q9XPJ8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 131.
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; ORFNames=DDB_G0294030;
OS   Dictyostelium discoideum (Social amoeba).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=8581739; DOI=10.1093/dnares/2.3.129;
RA   Iwamoto M., Yanagisawa K., Tanaka Y.;
RT   "Mitochondrial ribosomal protein L11 gene of Dictyostelium discoideum
RT   resides not in the nuclear genome but in the mitochondrial genome.";
RL   DNA Res. 2:129-132(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=10821186; DOI=10.1007/pl00008685;
RA   Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA   Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT   "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT   content and genome organization.";
RL   Mol. Gen. Genet. 263:514-519(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 34-45; 115-122; 238-246 AND 261-272, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH NDUFAF7.
RX   PubMed=20406883; DOI=10.1242/jcs.066076;
RA   Carilla-Latorre S., Gallardo M.E., Annesley S.J., Calvo-Garrido J.,
RA   Grana O., Accari S.L., Smith P.K., Valencia A., Garesse R., Fisher P.R.,
RA   Escalante R.;
RT   "MidA is a putative methyltransferase that is required for mitochondrial
RT   complex I function.";
RL   J. Cell Sci. 123:1674-1683(2010).
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; D21196; BAA04731.1; -; Genomic_DNA.
DR   EMBL; AB000109; BAA78067.1; -; Genomic_DNA.
DR   PIR; T43763; T43763.
DR   RefSeq; NP_050085.1; NC_000895.1.
DR   AlphaFoldDB; Q23883; -.
DR   SMR; Q23883; -.
DR   STRING; 44689.Q23883; -.
DR   GeneID; 2193913; -.
DR   KEGG; ddi:DidioMp18; -.
DR   dictyBase; DDB_G0294030; nad7.
DR   InParanoid; Q23883; -.
DR   OMA; IMGTSME; -.
DR   PhylomeDB; Q23883; -.
DR   Reactome; R-DDI-6799198; Complex I biogenesis.
DR   PRO; PR:Q23883; -.
DR   Proteomes; UP000002195; Mitochondrion.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; TIGR01962; NuoD; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW   Respiratory chain; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..406
FT                   /note="NADH-ubiquinone oxidoreductase 49 kDa subunit"
FT                   /id="PRO_0000118589"
SQ   SEQUENCE   406 AA;  46833 MW;  581BCF7AD71F86A8 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 YQSLSIIEQA LNNLRPGLIK
     LEGVNITAPD RAFVKKDMES CINHFKFFSE GFIIPANENY TIVEAPKGEF GIYLNANDTA
     KPYRCRIKAP GFLHLQGLNM MSKDHLLADV VTLIGTQDIV FGEVDR
//