NQO6_PARDE
ID NQO6_PARDE Reviewed; 173 AA.
AC P29918;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NADH-quinone oxidoreductase subunit 6;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit 6;
DE AltName: Full=NDH-1 subunit 6;
GN Name=nqo6;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=1637825; DOI=10.1021/bi00145a009;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "Gene cluster of the energy-transducing NADH-quinone oxidoreductase of
RT Paracoccus denitrificans: characterization of four structural gene
RT products.";
RL Biochemistry 31:6925-6932(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=[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 {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M93015; AAA03036.1; ALT_SEQ; Unassigned_DNA.
DR PIR; E42573; E42573.
DR AlphaFoldDB; P29918; -.
DR SMR; P29918; -.
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: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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Translocase; Ubiquinone.
FT CHAIN 1..173
FT /note="NADH-quinone oxidoreductase subunit 6"
FT /id="PRO_0000118762"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 173 AA; 19117 MW; 587B86578797CAEF CRC64;
MTGLNTAGAD RDLATAELNR ELQDKGFLLT TTEDIINWAR NGSLHWMTFG LACCAVEMMQ
TSMPRYDLER FGTAPRASPR QSDLMIVAGT LTNKMAPALR KVYDQMPEPR YVISMGSCAN
GGGYYHYSYS VVRGCDRIVP VDIYVPGCPP TAEALLYGIL QLQRRASGAP ARW