ID   NUOCD_RHOPB             Reviewed;         581 AA.
AC   Q20Z41;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01359};
DE   AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
DE   AltName: Full=NDH-1 subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01359};
GN   Synonyms=nuoCD {ECO:0000255|HAMAP-Rule:MF_01359},
GN   nuoD {ECO:0000255|HAMAP-Rule:MF_01359}; OrderedLocusNames=RPC_4069;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01359}.
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_01359};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01359}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01359}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
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DR   EMBL; CP000301; ABD89595.1; -; Genomic_DNA.
DR   RefSeq; WP_011474476.1; NC_007925.1.
DR   AlphaFoldDB; Q20Z41; -.
DR   SMR; Q20Z41; -.
DR   STRING; 316056.RPC_4069; -.
DR   EnsemblBacteria; ABD89595; ABD89595; RPC_4069.
DR   KEGG; rpc:RPC_4069; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_5; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01359; NDH1_NuoCD_1; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR023062; NADH_DH_suCD.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
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; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..581
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358676"
FT   REGION          1..172
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT   REGION          196..581
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ   SEQUENCE   581 AA;  65637 MW;  360F822F78DA9BB5 CRC64;
     MSAVELVNEL SARFGEAVFG EQPTHDAFPT LWIKPEAMPA LHRYLKHEIE RPFPLLVDLW
     AIDETARHHR EGQPPSGVTI ASHLMSLERN ADIRLKCALP ADDPRAHTIA EIYPNADWYE
     REAFDMFGVH FEGRRDHRRI LMPPLWDGHP MRKDQPARAT ERPPFVMTAA RFDAEEQALA
     VDPEALGLPT QRDGVELMIL NYGPHSMATH GVFRIVLALD GEEIVAARPD IGFHHRGAEK
     MGERQSWHQY IPYTDRIDYL GGVMGEMPYL QAVERLCGIA VPERAQTVRI MLCEIFRIMN
     HLLFYGTLAQ DTGAMSPVFY MFTDRERGYR VIEAITGARM HPGWFRIGGL AADLPEGWDA
     LVRDFLDWMP ARLDDYEGMV MRNEIFRART VGIAAYDTAT AFDWGITGPG LRATGCGWDM
     RKARPYGGYQ NFEFEVPTGH RGDCYDRARV RVDEIRQSLR IIRQCLDHMP AGPIKADHPL
     TTPPPRERML HDIETMIHHF VGSSWGPVVP VGEATGQVES VRGLTQYAVV SDGETTAYRT
     RIRTPSFAHL QSIATIAPGL TVADLVAYLG SIDYVMSDVD R