ID   NDUS8_RECAM             Reviewed;         162 AA.
AC   O21233;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=NADH-ubiquinone oxidoreductase subunit 8;
DE            EC=7.1.1.2;
GN   Name=NAD8;
OS   Reclinomonas americana.
OG   Mitochondrion.
OC   Eukaryota; Discoba; Jakobida; Histionina; Histionidae; Reclinomonas.
OX   NCBI_TaxID=48483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 50394;
RX   PubMed=9168110; DOI=10.1038/387493a0;
RA   Lang B.F., Burger G., O'Kelly C.J., Cedergren R., Golding G.B., Lemieux C.,
RA   Sankoff D., Turmel M., Gray M.W.;
RT   "An ancestral mitochondrial DNA resembling a eubacterial genome in
RT   miniature.";
RL   Nature 387:493-497(1997).
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). May donate electrons to ubiquinone. {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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF007261; AAD11860.1; -; Genomic_DNA.
DR   PIR; S78127; S78127.
DR   RefSeq; NP_044745.1; NC_001823.1.
DR   AlphaFoldDB; O21233; -.
DR   SMR; O21233; -.
DR   GeneID; 801137; -.
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   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   PANTHER; PTHR10849; PTHR10849; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Repeat; Respiratory chain; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..162
FT                   /note="NADH-ubiquinone oxidoreductase subunit 8"
FT                   /id="PRO_0000118718"
FT   DOMAIN          54..83
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          93..122
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   162 AA;  18662 MW;  0254DC6C0E54A724 CRC64;
     MTIINKTAQT LFLTELVKGM SLTLDYFFRK KVTLNYPFEK GPLSPRFRGE HALRRYQTGE
     ERCIACKLCE AICPAQAITI ESEPRIDGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG
     PNFEFATETH EELLYDKEKL LQNGDRWETE IAANLANEAL YR