ID   NQO5_PARDE              Reviewed;         207 AA.
AC   P29917;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=NADH-quinone oxidoreductase chain 5;
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NADH dehydrogenase I, chain 5;
DE   AltName: Full=NDH-1, chain 5;
GN   Name=nqo5;
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 2-15.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01357};
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 30 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR   EMBL; M93015; AAA03037.1; ALT_SEQ; Unassigned_DNA.
DR   PIR; D42573; D42573.
DR   RefSeq; WP_011748534.1; NZ_PPGA01000003.1.
DR   AlphaFoldDB; P29917; -.
DR   SMR; P29917; -.
DR   TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PRIDE; P29917; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW   NAD; Quinone; Translocase; Transport; Ubiquinone.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1637825"
FT   CHAIN           2..207
FT                   /note="NADH-quinone oxidoreductase chain 5"
FT                   /id="PRO_0000118668"
SQ   SEQUENCE   207 AA;  23731 MW;  070DFDEBE70FEC6D CRC64;
     MSEALSDEAL LELAEHIAVR RENDVISTQA VGELTVNATL SGVIGLIEFL RNDPNCRFST
     LIDITAVDNP ARPARFDVVY HLLSMYQNQR IRVKVQVRED ELVPSLIGVF PGANWYEREV
     FDLFGILFSG HSDLRRILTD YGFRGHPLRK DFPTTGYVEV RWSDIEKRVV YEPVNLVQEY
     RQFDFLSPWE GAKYVLPGDE KAPEAKK