NDUV2_CAEEL
ID NDUV2_CAEEL Reviewed; 239 AA.
AC Q20719;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE Flags: Precursor;
GN ORFNames=F53F4.10;
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).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a
CC component of the flavoprotein-sulfur (FP) fragment of the enzyme (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; Z77663; CAB01203.1; -; Genomic_DNA.
DR PIR; T22573; T22573.
DR RefSeq; NP_506376.1; NM_073975.6.
DR AlphaFoldDB; Q20719; -.
DR SMR; Q20719; -.
DR BioGRID; 44866; 38.
DR DIP; DIP-26781N; -.
DR IntAct; Q20719; 1.
DR STRING; 6239.F53F4.10; -.
DR World-2DPAGE; 0020:Q20719; -.
DR EPD; Q20719; -.
DR PaxDb; Q20719; -.
DR PeptideAtlas; Q20719; -.
DR EnsemblMetazoa; F53F4.10.1; F53F4.10.1; WBGene00009992.
DR GeneID; 179850; -.
DR KEGG; cel:CELE_F53F4.10; -.
DR UCSC; F53F4.10.1; c. elegans.
DR CTD; 179850; -.
DR WormBase; F53F4.10; CE10972; WBGene00009992; -.
DR eggNOG; KOG3196; Eukaryota.
DR GeneTree; ENSGT00390000017580; -.
DR HOGENOM; CLU_054362_1_0_1; -.
DR InParanoid; Q20719; -.
DR OMA; VGKFHVQ; -.
DR OrthoDB; 1396088at2759; -.
DR PhylomeDB; Q20719; -.
DR PRO; PR:Q20719; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00009992; Expressed in embryo and 4 other tissues.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:WormBase.
DR GO; GO:0051537; F:2 iron, 2 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; IEA:UniProtKB-EC.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transport; Ubiquinone.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..239
FT /note="Probable NADH dehydrogenase [ubiquinone]
FT flavoprotein 2, mitochondrial"
FT /id="PRO_0000020006"
FT REGION 200..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 165
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 169
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 26241 MW; 2A63223AFE663E91 CRC64;
MSLASNVLLQ ASRLGEMVIK RGGATGLMVH RDTKENNLNV KFKFTSENQE RIKAIMDIYP
EGHKAGALIP LLDLAQRQHG WLPISAMHEV AKILEVPRMR AYEVATFYTM FNRQPVGKYF
LQVCATTPCM LRGAETITET IEKKLGIHAG ETTKDGLFTL AEVECLGACV NAPMIQINDD
YFEDLTPKDV NEILDDLKAG RKPAAGPRSG RLAAEPFGEL TSLKETPPGP GFGLQAALK
