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 25-NOV-2008, entry version 58. DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit; DE AltName: Full=Complex I-20kD; DE Short=CI-20kD; DE Flags: Precursor; GN ORFNames=W10D5.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] 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 1 4Fe-4S cluster (Potential). 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 20 kDa subunit family. 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; Z79758; CAB02132.1; -; Genomic_DNA. DR PIR; T26329; T26329. DR RefSeq; NP_492445.1; -. DR UniGene; Cel.18304; -. DR Ensembl; W10D5.2; Caenorhabditis elegans. DR GeneID; 172734; -. DR KEGG; cel:W10D5.2; -. DR WormBase; WBGene00012376; W10D5.2. DR WormPep; W10D5.2; CE14780. DR NextBio; 876791; -. DR ArrayExpress; Q94360; -. DR GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to u...; IEA:InterPro. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0040018; P:positive regulation of multicellular organi...; IMP:WormBase. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR006138; NADH_DHase_20kDa_su. DR InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB. DR InterPro; IPR006137; OxRdtase_q6. DR PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1. DR PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 2: Evidence at transcript level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 199 Probable NADH dehydrogenase [ubiquinone] FT iron-sulfur protein 7, mitochondrial. FT /FTId=PRO_0000020030. FT METAL 74 74 Iron-sulfur (4Fe-4S) (Potential). FT METAL 75 75 Iron-sulfur (4Fe-4S) (Potential). FT METAL 139 139 Iron-sulfur (4Fe-4S) (Potential). FT METAL 169 169 Iron-sulfur (4Fe-4S) (Potential). 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 //