ID   NQO9_RHOMR              Reviewed;         230 AA.
AC   Q4QSC5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   04-NOV-2026, entry version 93.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 9;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit 9;
DE   AltName: Full=NDH-1 subunit 9;
GN   Name=nqo9;
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia; Rhodothermales;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRQ 62B;
RX   PubMed=16023073; DOI=10.1016/j.bbabio.2005.06.003;
RA   Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M.,
RA   Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.;
RT   "A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus
RT   marinus complex I genes.";
RL   Biochim. Biophys. Acta 1709:95-103(2005).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       menaquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124;
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   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits Nqo7-14
CC       constitute the membrane sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AY972099; AAY42993.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4QSC5; -.
DR   SMR; Q4QSC5; -.
DR   OMA; AALWMIC; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) (non-electrogenic) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
DR   Gene3D; 3.30.70.3270; -; 1.
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   NCBIfam; TIGR01971; NuoI; 1.
DR   PANTHER; PTHR10849:SF35; FORMATE HYDROGENLYASE SUBUNIT 6-RELATED; 1.
DR   PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Quinone; Repeat; Translocase.
FT   CHAIN           1..230
FT                   /note="NADH-quinone oxidoreductase subunit 9"
FT                   /id="PRO_0000245739"
FT   DOMAIN          60..93
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          104..133
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  27120 MW;  E951770E49179E57 CRC64;
     MPGKPVNLAS PNERKLNFWE RLYLPAVVQG LAYTWRKMRS PRYTFQYPDE LWYPPDSYRG
     RPVLVEENGR PRCVACGLCA RACPPLAISM QAKEVDDVKE REPAWFEINM LRCIYCGYCE
     EVCPEEAIVM SKEYDLTFQS RDEAIFGLEK LLVPAERLKD RLEWLDRYKD PQYGQHWEFR
     KENNLHSLKD RPFLKWLLEE EGMEELKSTH LRPEEPVAAE RSWGGVRAEG
//