ID   NQO4_PARDE              Reviewed;         412 AA.
AC   P29916;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 4;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I, subunit 4;
DE   AltName: Full=NDH-1, subunit 4;
GN   Name=nqo4;
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 1-15.
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   -!- 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 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M93015; AAA03038.1; -; Unassigned_DNA.
DR   PIR; F42573; F42573.
DR   AlphaFoldDB; P29916; -.
DR   SMR; P29916; -.
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:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW   NAD; Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..412
FT                   /note="NADH-quinone oxidoreductase subunit 4"
FT                   /id="PRO_0000118616"
SQ   SEQUENCE   412 AA;  46674 MW;  A3299D2E54011296 CRC64;
     MDGDIRKNSL DDGSMDALTG EQSIRNFNIN FGPQHPAAHG LLRMVLELDG EIVERADPHI
     GLLHRGTEKL MESRTYLQNL PYLDRLDYVA PMNQEHAWCL AIERLTGTVI PRRASLIRVL
     YSEIGRILNH LMGVTTGAMD VGALTPPLWG FEAREELMIF YERACGARLH AAYFRPGGVH
     QDLPPDLLDD IEEWCERFPK LVDDLDTLLT ENRIFKQRLV DIGIVTEADA LDWGYTGVMV
     RGSGLAWDLR RSQPYECYDE FDFQIPVGRN GDCYDRYLCR MAEMRESCKI MQQAVQKLRA
     EPAGDVLARG KLTPPRRAEM KRDMESLIHH FKLYTEGFKV PAGEVYAAVE GPKGEFGVYL
     VADGTNKPWR AKLRAPGFAH LQSIDWMSRG HMLADVPAII ATLDIVFGEV DR