NQO1_PARDE
ID NQO1_PARDE Reviewed; 431 AA.
AC P29913;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NADH-quinone oxidoreductase chain 1;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I, chain 1;
DE AltName: Full=NDH-1, chain 1;
GN Name=nqo1;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-37.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=1905152; DOI=10.1021/bi00240a012;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "The NADH-binding subunit of the energy-transducing NADH-ubiquinone
RT oxidoreductase of Paracoccus denitrificans: gene cloning and deduced
RT primary structure.";
RL Biochemistry 30:6422-6428(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND PROTEIN SEQUENCE OF 1-37 AND
RP 194-203.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=1909571; DOI=10.1021/bi00099a027;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "Characterization of the 25-kilodalton subunit of the energy-transducing
RT NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence
RT similarity to the 24-kilodalton subunit of the flavoprotein fraction of
RT mammalian complex I.";
RL Biochemistry 30:8678-8684(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 416-431.
RX PubMed=1605643; DOI=10.1016/0003-9861(92)90542-5;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "Structural features of the 66-kDa subunit of the energy-transducing NADH-
RT ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans.";
RL Arch. Biochem. Biophys. 296:40-48(1992).
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 ubiquinone. 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.
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=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, Nqo1 to
CC Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M64432; AAA25585.1; -; Genomic_DNA.
DR PIR; A39588; A39588.
DR AlphaFoldDB; P29913; -.
DR SMR; P29913; -.
DR TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Translocase; Ubiquinone.
FT CHAIN 1..431
FT /note="NADH-quinone oxidoreductase chain 1"
FT /id="PRO_0000118566"
FT BINDING 54..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 167..214
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 349
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 392
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 431 AA; 47191 MW; AA25C5A0A7570048 CRC64;
MLNDQDRIFT NLYGMGDRSL AGAKKRGHWD GTAAIIQRGR DKIIDEMKAS GLRGRGGAGF
PTGMKWSFMP KESDGRPSYL VINADESEPA TCKDREIMRH DPHTLIEGAL IASFAMGAHA
AYIYIRGEFI REREALQAAI DECYDAGLLG RNAAGSGWDF DLYLHHGAGA YICGEETALL
ESLEGKKGMP RMKPPFPAGA GLYGCPTTVN NVESIAVVPT ILRRGAEWFA SFGRPNNAGV
KLFGLTGHVN TPCVVEEAMS IPMRELIEKH GGGIRGGWKN LKAVIPGGAS CPVLTAEQCE
NAIMDYDGMR DVRSSFGTAC MIVMDQSTDV VKAIWRLSKF FKHESCGQCT PCREGTGWMM
RVMERLVRGD AEVEEIDMLF DVTKQVEGHT ICALGDAAAW PIQGLIRNFR EEIEDRIKAK
RTGRMGAMAA E
