NDUS7_CAEEL
ID NDUS7_CAEEL Reviewed; 199 AA.
AC Q94360;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-20kD;
DE Short=CI-20kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE Flags: Precursor;
GN Name=nduf-7; ORFNames=W10D5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
RX PubMed=12853115; DOI=10.1016/s0925-4439(03)00079-6;
RA Tsang W.Y., Lemire B.D.;
RT "The role of mitochondria in the life of the nematode, Caenorhabditis
RT elegans.";
RL Biochim. Biophys. Acta 1638:91-105(2003).
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). {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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits This is a
CC component of the iron-sulfur (IP) fragment of the enzyme.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 20 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; Z79758; CAB02132.1; -; Genomic_DNA.
DR PIR; T26329; T26329.
DR RefSeq; NP_492445.1; NM_060044.4.
DR AlphaFoldDB; Q94360; -.
DR SMR; Q94360; -.
DR BioGRID; 38165; 42.
DR STRING; 6239.W10D5.2.1; -.
DR EPD; Q94360; -.
DR PaxDb; Q94360; -.
DR PeptideAtlas; Q94360; -.
DR PRIDE; Q94360; -.
DR EnsemblMetazoa; W10D5.2.1; W10D5.2.1; WBGene00012376.
DR EnsemblMetazoa; W10D5.2.2; W10D5.2.2; WBGene00012376.
DR GeneID; 172734; -.
DR KEGG; cel:CELE_W10D5.2; -.
DR CTD; 172734; -.
DR WormBase; W10D5.2; CE14780; WBGene00012376; nduf-7.
DR eggNOG; KOG1687; Eukaryota.
DR GeneTree; ENSGT00390000006565; -.
DR HOGENOM; CLU_055737_1_2_1; -.
DR InParanoid; Q94360; -.
DR OMA; GPYWEHG; -.
DR OrthoDB; 1278656at2759; -.
DR PhylomeDB; Q94360; -.
DR Reactome; R-CEL-6799198; Complex I biogenesis.
DR PRO; PR:Q94360; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00012376; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:WormBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IC:WormBase.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..199
FT /note="Probable NADH dehydrogenase [ubiquinone] iron-sulfur
FT protein 7, mitochondrial"
FT /id="PRO_0000020030"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 199 AA; 21912 MW; B40B33385A7DB667 CRC64;
MLSALRTAGA VGTRRLASTQ AIASNSEAPK GIATTGTPFL NPSSKAEYAL ARLDDVLNLA
QRGSIWPLTF GLACCAVEMM HFAAPRYDMD RYGVVFRASP RQADLIFVAG TVTNKMAPAL
RRIYDQMPEA KWVISMGSCA NGGGYYHYAY SVLRGCDRVI PVDIYVPGCP PTAEALLYGV
LQLQKKIKRK REAQLWYRR
