NDUS7_CAEBR
ID NDUS7_CAEBR Reviewed; 199 AA.
AC A8XFG2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial {ECO:0000250|UniProtKB:Q94360};
DE EC=7.1.1.2;
DE Flags: Precursor;
GN Name=nduf-7 {ECO:0000312|EMBL:CAP31423.1}; ORFNames=CBG12445;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP31423.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(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|UniProtKB:P42026}.
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 Evidence={ECO:0000250|UniProtKB:Q94360};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255};
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|UniProtKB:P42026}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P42026}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255}.
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DR EMBL; HE600913; CAP31423.1; -; Genomic_DNA.
DR RefSeq; XP_002639719.1; XM_002639673.1.
DR AlphaFoldDB; A8XFG2; -.
DR SMR; A8XFG2; -.
DR STRING; 6238.CBG12445; -.
DR EnsemblMetazoa; CBG12445.1; CBG12445.1; WBGene00033393.
DR GeneID; 8581712; -.
DR KEGG; cbr:CBG_12445; -.
DR CTD; 8581712; -.
DR WormBase; CBG12445; CBP03002; WBGene00033393; Cbr-nduf-7.
DR eggNOG; KOG1687; Eukaryota.
DR HOGENOM; CLU_055737_1_2_1; -.
DR InParanoid; A8XFG2; -.
DR OMA; GPYWEHG; -.
DR OrthoDB; 1278656at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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: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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..199
FT /note="Probable NADH dehydrogenase [ubiquinone] iron-sulfur
FT protein 7, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395332"
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; 21975 MW; D617BEE4605514C5 CRC64;
MLSALRTAGA LSTRRLASTQ AIASNSEAPK GIATTGTPFL NPSSKAEYAL ARLDDVMNLA
QRGSIWPLTF GLACCAVEMM HFAAPRYDMD RYGVVFRASP RQADLIFVAG TVTNKMAPAL
RRIYDQMPEA KWVISMGSCA NGGGYYHYAY SVLRGCDRVI PVDIYVPGCP PTAEALLYGV
LQLQKKIKRK REAQLWYRR
