NDUS7_PARTE
ID NDUS7_PARTE Reviewed; 156 AA.
AC P15602; Q35365;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE EC=7.1.1.2;
GN Name=NAD10; Synonyms=PSBG;
OS Paramecium tetraurelia.
OG Mitochondrion.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock 51;
RX PubMed=2308823; DOI=10.1093/nar/18.1.173;
RA Pritchard A.E., Seilhamer J.J., Mahalingam R., Sable C.L., Venuti S.E.,
RA Cummings D.J.;
RT "Nucleotide sequence of the mitochondrial genome of Paramecium.";
RL Nucleic Acids Res. 18:173-180(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock 51;
RX PubMed=2670676; DOI=10.1016/0378-1119(89)90320-x;
RA Pritchard A.E., Venuti S.E., Ghalambor M.A., Sable C.L., Cummings D.J.;
RT "An unusual region of Paramecium mitochondrial DNA containing chloroplast-
RT like genes.";
RL Gene 78:121-134(1989).
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 -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X15917; CAA34045.1; -; Genomic_DNA.
DR EMBL; M26930; AAA79257.1; -; Genomic_DNA.
DR PIR; S07736; F2PPG.
DR AlphaFoldDB; P15602; -.
DR SMR; P15602; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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; Respiratory chain; Translocase;
KW Transport.
FT CHAIN 1..156
FT /note="NADH-ubiquinone oxidoreductase 20 kDa subunit"
FT /id="PRO_0000118739"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT CONFLICT 123..127
FT /note="MLCPR -> IFVPG (in Ref. 2; AAA79257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17454 MW; B056E34343D75C2F CRC64;
MILKADFLKL SANNLISWAR QGSFWPLTFG LACCALEMMH ATVSRYDFDR FGVIFRATPR
QADLIIVAGT VTNKMAPALR RLYDQTADPK WVLSMGSCAN GGGYYHYSYA VVKGCDKIIP
VDMLCPRCPP TAEALFFGVL QLQKTLMKTI NEKKVF