NQO9_RHOMR
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 03-AUG-2022, entry version 80.
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; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
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 + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, 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 GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
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; 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
