ID   NQO13_PARDE             Reviewed;         513 AA.
AC   P29925;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=NADH-quinone oxidoreductase chain 13;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I, chain 13;
DE   AltName: Full=NDH-1, chain 13;
GN   Name=nqo13 {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].
RC   STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
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).
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; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; L02354; AAA25599.1; -; Genomic_DNA.
DR   PIR; I45456; I45456.
DR   AlphaFoldDB; P29925; -.
DR   SMR; P29925; -.
DR   TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR43507; PTHR43507; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN           1..513
FT                   /note="NADH-quinone oxidoreductase chain 13"
FT                   /id="PRO_0000118037"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   513 AA;  56417 MW;  8164DEACA20FE739 CRC64;
     MTNLLSIITF LPIVAAIIMA LFLRGQDEAA ARNAKWLALL TTTATFVISL FVLFRFDPAN
     TGFQFVEDHA WIMGVCYKMG VDGISVLFVL LTTFMMPLTI LSTWQVQDKV KEYMIAFLVL
     EGLMIGVFTA LDLVLFYLFF EAGLIPMFLI IGIWGGKDRI YASFKFFLYT FLGSVLMLVA
     MIAMYRMAGT TDIPTLLTFD FPSENFRLLG MTVVGGMQML LFLAFFASFA VKMPMWPVHT
     WLPDAHVQAP TAGSVLLAAV LLKMGGYGFL RFSLPMFPVA SGVAQPYVFW LSAIAIVYTS
     LVALAQSDMK KVIAYSSVAH MGYVTMGVFA ANQIGVDGAI FQMLSHGFIS GALFLCVGVI
     YDRMHTREID AYGGLVNRMP AYAAVFMFFT MANVGLPGTS GFVGEFLTLM GVFRVDTWVA
     LVATSGVILS AAYALWLYRR VTLGQLIKES LKSITDMTPR ERWVFIPLIA MTLILGVYPR
     LVTDVTGPAV AALVQDYNQS QPAAPVATAQ ASH