NQO3_PARDE
ID NQO3_PARDE Reviewed; 673 AA.
AC P29915;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=NADH-quinone oxidoreductase chain 3;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I, chain 3;
DE AltName: Full=NDH-1, chain 3;
GN Name=nqo3 {ECO:0000303|PubMed:8422400};
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 2-16.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-673.
RX PubMed=8422400; DOI=10.1021/bi00054a030;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "DNA sequencing of the seven remaining structural genes of the gene cluster
RT encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus
RT denitrificans.";
RL Biochemistry 32:968-981(1993).
RN [3]
RP IDENTIFICATION OF A [2FE--2S] AND A [4FE--4S] CLUSTER, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7629145; DOI=10.1074/jbc.270.31.18264;
RA Yano T., Yagi T., Sled' V.D., Ohnishi T.;
RT "Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur
RT subunit of the proton-translocating NADH-quinone oxidoreductase of
RT Paracoccus denitrificans.";
RL J. Biol. Chem. 270:18264-18270(1995).
RN [4]
RP IDENTIFICATION OF A SECOND [4FE--4S] CLUSTER, AND MUTAGENESIS OF HIS-106.
RX PubMed=12600982; DOI=10.1074/jbc.m212275200;
RA Yano T., Sklar J., Nakamaru-Ogiso E., Takahashi Y., Yagi T., Ohnishi T.;
RT "Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the
RT Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase
RT from Paracoccus denitrificans.";
RL J. Biol. Chem. 278:15514-15522(2003).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:7629145};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is
CC known as N1b. {ECO:0000269|PubMed:7629145};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:12600982, ECO:0000269|PubMed:7629145};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. The [4Fe-4S] cluster 1 is
CC known as N5 and [4Fe-4S] cluster 3 as N4. {ECO:0000269|PubMed:12600982,
CC ECO:0000269|PubMed:7629145};
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 {ECO:0000305|PubMed:7629145}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M84572; AAA25587.1; -; Genomic_DNA.
DR PIR; S23948; A45456.
DR AlphaFoldDB; P29915; -.
DR SMR; P29915; -.
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:0051537; F:2 iron, 2 sulfur cluster binding; 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:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NuoG_C.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Translocase; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1605643"
FT CHAIN 2..673
FT /note="NADH-quinone oxidoreductase chain 3"
FT /id="PRO_0000118540"
FT DOMAIN 5..90
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 90..129
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 227..283
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000305|PubMed:12600982"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MUTAGEN 106
FT /note="H->A: Very little incorporation of iron-sulfur
FT centers into protein in E.coli."
FT /evidence="ECO:0000269|PubMed:12600982"
FT MUTAGEN 106
FT /note="H->C: Alters the EPR signal of the N5 cluster; all 3
FT iron-sulfur clusters are less stable in E.coli."
FT /evidence="ECO:0000269|PubMed:12600982"
SQ SEQUENCE 673 AA; 73159 MW; 5778B4A77940CF1D CRC64;
MADLRKIKID DTIIEVDPNM TLIQACEMAG IEVPRFCYHE RLSIAGNCRM CLVEVVGGPP
KPAASCAMQV KDLRPGPEGA PSEIRTNSPM VKKAREGVME FLLINHPLDC PICDQGGECD
LQDQAMAYGV DFSRYREPKR ATEDLNLGPL VETHMTRCIS CTRCVRFTTE VAGITQMGQT
GRGEDSEITS YLNQTLESNM QGNIIDLCPV GALVSKPYAF TARPWELTKT ESIDVMDALG
SSIRIDTKGR EVMRILPRNH DGVNEEWISD KTRFVWDGLR RQRLDRPYIR ENGRLRPASW
PEALEAAARA MKGKKIAGLI GDLVPAEAAF SLKQLVEGLG GKVECRVDGA RLPAGNRSAY
VGTARIEDID DAEMIQLIGT NPRDEAPVLN ARIRKAWSKG AKVGLVGEPV DLTYDYAHVG
TDRAALESLS SREISDETKA RPSIVIVGQG AIARRDGEAV LAHAMKLAEN SNSGLLILHT
AAGRVGAMDV GAVTEGGLLA AIDGAEVVYN LGADEVDIDQ GPFVIYQGSH GDRGAHRDII
LPGACYTEES GLFVNTEGRP QLAMRANFAP GEGKENWAIL RALSAELGAT QPWDSLAGLR
RKLVEAVPHL AQIDQVPQNE WQPLGRFDLG QASFRYAIRD FYLTNPIARS SPLMGELSAM
AAARKAPAPL AAE
