ID   NUOCD_HALVD             Reviewed;         557 AA.
AC   D4GVF7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit C/D;
DE   AltName: Full=NDH-1 subunit C/D;
GN   Name=nuoCD; OrderedLocusNames=HVO_0980;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   SAMPYLATION AT LYS-517, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20054389; DOI=10.1038/nature08659;
RA   Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA   Chen S., Wells L., Maupin-Furlow J.A.;
RT   "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT   volcanii.";
RL   Nature 463:54-60(2010).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
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 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000305}.
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DR   EMBL; CP001956; ADE04185.1; -; Genomic_DNA.
DR   RefSeq; WP_004043963.1; NZ_AOHU01000092.1.
DR   AlphaFoldDB; D4GVF7; -.
DR   SMR; D4GVF7; -.
DR   STRING; 309800.C498_13864; -.
DR   EnsemblBacteria; ADE04185; ADE04185; HVO_0980.
DR   GeneID; 8926295; -.
DR   KEGG; hvo:HVO_0980; -.
DR   eggNOG; arCOG01548; Archaea.
DR   HOGENOM; CLU_015134_3_2_2; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 4328at2157; -.
DR   Proteomes; UP000008243; Chromosome.
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   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; IPR020396; NADH_UbQ_OxRdtase_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   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Isopeptide bond; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Reference proteome; Translocase; Transport; Ubl conjugation.
FT   CHAIN           1..557
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000397108"
FT   REGION          1..174
FT                   /note="NADH dehydrogenase I subunit C"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..557
FT                   /note="NADH dehydrogenase I subunit D"
FT   CROSSLNK        517
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP2)"
FT                   /evidence="ECO:0000269|PubMed:20054389"
SQ   SEQUENCE   557 AA;  63484 MW;  7D1CD97F83740243 CRC64;
     MSLEEQQSDD PAELESGVSR GDELAELLGD LVVGREEHLN APGLVIRPDE VQDALFKLRD
     EAGFDHLSCV TAQEYEDRYE SIYHLTKFDD RTDEVSVVVP TSKDNPVSQS AEPVFRTADW
     HEREAYDLVG IQYEDHPDLR RILLPETWQG HPLGLDYDQD RPQIATLREH ANPLEEDHRA
     GDSNTMYINI GPHHPATHGV LHVETVVDGE QVVDLESDIG YLHRCEEQMC QQGTYRHQIM
     PYPDRWDYIS SGLLNEWAYA RAAEDLADIE VPEYAQIIRT MGAELCRIAS HMIALGTFAL
     DVYGDFTAIF MYAMRDREIV QNILEDLTGQ RMMFNYFRLG GVVWDLPEPR EEFFEKIRDF
     MDGLPQALEE YHDMITSNEI LQARTVGTGV LSPEVAKSYG ATGPVARGSG IDYDLRRDDS
     YGYYDELEWD VVVEDGCDNF SRLLVRMREV EESAKIIQQC VDLLEDWPED ERNIQANVPR
     TLKPDEDTEI YRAVEGAKGE LGIYIRADGT DKPARFKIRS PCFSNLQTLP EMSEGEYIPD
     MIASLGSLDI VLGEVDR