ID   NUOD_CERS4              Reviewed;         404 AA.
AC   Q3J3F8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=RHOS4_11080;
GN   ORFNames=RSP_2515;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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_01358}.
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_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000143; ABA78676.1; -; Genomic_DNA.
DR   RefSeq; WP_011337547.1; NZ_CP030271.1.
DR   RefSeq; YP_352577.1; NC_007493.2.
DR   AlphaFoldDB; Q3J3F8; -.
DR   SMR; Q3J3F8; -.
DR   STRING; 272943.RSP_2515; -.
DR   EnsemblBacteria; ABA78676; ABA78676; RSP_2515.
DR   GeneID; 57469857; -.
DR   KEGG; rsp:RSP_2515; -.
DR   PATRIC; fig|272943.9.peg.1436; -.
DR   eggNOG; COG0649; Bacteria.
DR   OMA; IMGTSME; -.
DR   PhylomeDB; Q3J3F8; -.
DR   Proteomes; UP000002703; Chromosome 1.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..404
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357898"
SQ   SEQUENCE   404 AA;  46056 MW;  CA05FFEE00A329D9 CRC64;
     MAMDTKFDDV LTGEQKLRNF NINFGPQHPA AHGVLRLVLE LDGEVVERCD PHIGLLHRGT
     EKLMESRTYL QNLPYFDRLD YVAPMNQEHA WCLAIERLTG VAVPRRASLI RVLYSEIGRV
     LNHLLNVTTQ AMDVGALTPP LWGFEEREKL MVFYERASGA RLHAAYFRPG GVHQDLTPRL
     IEDIEEWAEH FPKVLDDLDE LLTENRIFKQ RNVDIGIISE KDILDWGFSG VMVRGSGFAW
     DLRRSQPYEC YDEFDFQIPV GKNGDCYDRY LCRMEEMRQS TRIIQQCLAK LRVEKGDVLA
     RGKLTPPPRG EMKTSMEALI HHFKLYTEGF HVPAGEVYAA VEAPKGEFGV YLVADGTNRP
     YRAKIRAPGF LHLQAIDYIA KGHLLADVSA IIGTLDVVFG EIDR