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 13-SEP-2023, entry version 68. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 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 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 //