ID NDUS8_CAEEL Reviewed; 212 AA. AC Q22619; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 76. DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit; DE AltName: Full=Complex I-23kD; DE Short=CI-23kD; DE Flags: Precursor; GN ORFNames=T20H4.5; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Bristol N2; RX MEDLINE=99377169; PubMed=10446229; DOI=10.1093/nar/27.17.3424; RA Hough R.F., Lingam A.T., Bass B.L.; RT "Caenorhabditis elegans mRNAs that encode a protein similar to ADARs RT derive from an operon containing six genes."; RL Nucleic Acids Res. 27:3424-3432(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity). CC -!- SUBUNIT: Complex I is composed of 45 different subunits This is a CC component of the iron-sulfur (IP) fragment of the enzyme (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF140272; AAD34863.1; -; mRNA. DR EMBL; U00037; AAA50662.1; -; Genomic_DNA. DR PIR; T16914; T16914. DR RefSeq; NP_498595.1; -. DR UniGene; Cel.34232; -. DR HSSP; P00198; 2FDN. DR DIP; DIP:24953N; -. DR IntAct; Q22619; 3. DR Ensembl; T20H4.5; Caenorhabditis elegans. DR GeneID; 176023; -. DR KEGG; cel:T20H4.5; -. DR NMPDR; fig|6239.3.peg.10480; -. DR WormBase; WBGene00020636; T20H4.5. DR WormPep; T20H4.5; CE00832. DR OMA; Q22619; DFFRINF. DR BRENDA; 1.6.5.3; 672. DR BRENDA; 1.6.99.3; 672. DR NextBio; 890788; -. DR ArrayExpress; Q22619; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0040007; P:growth; IMP:WormBase. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR Pfam; PF00037; Fer4; 2. DR TIGRFAMs; TIGR01971; NuoI; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 2: Evidence at transcript level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Repeat; KW Respiratory chain; Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 ? Mitochondrion (By similarity). FT CHAIN ? 212 Probable NADH dehydrogenase [ubiquinone] FT iron-sulfur protein 8, mitochondrial. FT /FTId=PRO_0000020015. FT DOMAIN 104 133 4Fe-4S ferredoxin-type 1. FT DOMAIN 143 172 4Fe-4S ferredoxin-type 2. FT METAL 113 113 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 116 116 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 119 119 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 123 123 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 152 152 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 155 155 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 158 158 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 162 162 Iron-sulfur 1 (4Fe-4S) (By similarity). SQ SEQUENCE 212 AA; 23870 MW; F50C413D89E80AB7 CRC64; MAMKSVAVLT KGMFGRIPAQ LAVSSVPSNT IQKRSNYKFV GMPNETDGTL AGDLNYGLHN VFFTELFRGF GVMLGHVFME PATINYPFEK GPLSSRFRGE HALRRYPSGE ERCIACKLCE AICPAQAITI EAETRPDGSR RTTRYDIDMT KCIYCGLCQE ACPVDAIVEG PNFEYSTETH EELLYNKEKL LLNGDRWEPE LASNLQAEYL YR //