NUOD_CHLCH
ID NUOD_CHLCH Reviewed; 400 AA.
AC Q3ASW5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-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=Cag_0637;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-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 a
CC menaquinone. 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}.
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DR EMBL; CP000108; ABB27910.1; -; Genomic_DNA.
DR RefSeq; WP_011361682.1; NC_007514.1.
DR AlphaFoldDB; Q3ASW5; -.
DR SMR; Q3ASW5; -.
DR STRING; 340177.Cag_0637; -.
DR EnsemblBacteria; ABB27910; ABB27910; Cag_0637.
DR KEGG; cch:Cag_0637; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_10; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
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; 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.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transport.
FT CHAIN 1..400
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000357794"
SQ SEQUENCE 400 AA; 44792 MW; 6DEF32BF98843756 CRC64;
MQELEKAVPS SVRVTRQSEN LVILEKDLAT EQMVLAMGPQ HPSTHGVLKL ECLTDGEVVT
EAEPVLGYLH RCFEKTAENV DYPAVVPFTD RLDYLAAMNS EFAYALTVEK LLDIEIPRRV
EFIRILVAEL NRIASHLVAI GTYGIDLGAF TPFLFCFRDR EIILGLLEWA SGARMLYNYV
WVGGLAYDVP ADFLKRIREF CAYFRPKAKE LADLLTSNEI FVKRTHGIGI MPADVAINYG
WSGPMLRGSG VEWDLRRNDP YSLYSELDFN VCVPDGKHSV IGDCLSRHLV RAYEMEESLN
IIEQCIDKMP SSDGFNSRAA IPKKIRPKAG EVYGRAENPR GELGFYIQSD GKSTKPLRCK
ARSSCFVNLS AMKDLSKGQL IPDLVAIIGS IDIVLGEVDR