ID   NUOD1_CYTH3             Reviewed;         392 AA.
AC   Q11XR6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D 1 {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD1 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=CHU_0512;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG57800.1; -; Genomic_DNA.
DR   RefSeq; WP_011583916.1; NZ_FPJX01000001.1.
DR   AlphaFoldDB; Q11XR6; -.
DR   SMR; Q11XR6; -.
DR   STRING; 269798.CHU_0512; -.
DR   EnsemblBacteria; ABG57800; ABG57800; CHU_0512.
DR   KEGG; chu:CHU_0512; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_10; -.
DR   OMA; TFAECIE; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000001822; Chromosome.
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;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..392
FT                   /note="NADH-quinone oxidoreductase subunit D 1"
FT                   /id="PRO_0000357802"
SQ   SEQUENCE   392 AA;  44600 MW;  36945562FAD24A06 CRC64;
     MESSEPLVLD VGNLKRGEII INMGPQHPST HGVLRLEILT DGEIVKDVIP HMGYLHRCYE
     KHAEKLPYNQ VIPFVDRMDY LAAMNSEHAY AMGVERMLGI ENDIPKRVEY IRVLVAELNR
     ISSHFVAIGT YGLDIGAFTP FLWVMRDREH INRLLEWVSG ARMLYNYIWV GGLFYDLPVG
     FEERCKDFIS YLKPKLAELQ KVIIDNKIFI ERTANIGVLP LDLAINYGIT GPMLRASGLK
     FDLRKVDAYS VYPEIDFDIP VGTGAVGTTG DCWDRTHVRV AECFESVKII EQCLEKLLGE
     HKRTREFDPQ AIVPKKIRPK VMDFYVRAEN PKGELGFFFR TTGNTDIPFR CKVRAPSFVN
     LSVLQAISKN VMIADLVAIL GSFDIVMGEI DR