NUOCD_CERS4
ID NUOCD_CERS4 Reviewed; 580 AA.
AC Q3J1Q7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=RHOS4_17090;
GN ORFNames=RSP_0102;
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_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; CP000143; ABA79277.1; -; Genomic_DNA.
DR RefSeq; WP_011337994.1; NZ_AKVW01000001.1.
DR RefSeq; YP_353178.1; NC_007493.2.
DR AlphaFoldDB; Q3J1Q7; -.
DR SMR; Q3J1Q7; -.
DR STRING; 272943.RSP_0102; -.
DR EnsemblBacteria; ABA79277; ABA79277; RSP_0102.
DR KEGG; rsp:RSP_0102; -.
DR PATRIC; fig|272943.9.peg.2042; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR OMA; GGRMHYM; -.
DR PhylomeDB; Q3J1Q7; -.
DR Proteomes; UP000002703; Chromosome 1.
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; Reference proteome; Translocase; Transport; Ubiquinone.
FT CHAIN 1..580
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000358671"
FT REGION 1..171
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT REGION 195..580
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ SEQUENCE 580 AA; 65341 MW; 1A3CC9A10896EEAB CRC64;
MSLDQAIPEA LQALRTRFGA AVRAEQATGE AFPVLWLDAS VWEAAHRFLR EEIAAPFPLL
ADLWAIDESL RQHRTGQPAS RITLCSHLVS LVRNADLRLK LATDGRAPSI AGVYANADWY
EREAHDMFGL DFGRETRRIL MPPTWEGHPL LKTHYARATE KPPFVLTDRL FEAEERATIT
DPDLLGLPKL RDGEELMVLN FGPHHPSTHG VLRILLGLDG EEVVWAWPDI GYHHRGAEKM
AERQTWHGFI PYCDRIDYLG GVISELPYLL AVERLCGIAV PPRAQMIRVM LCEFYRIMNH
LLFYGTMAQD VGAMSPVFYM FTDREKGHEI LNAITGARMH PAFFRIGGVA MDLPDGWDAM
VRGFLDWMPA RLDEYERMVL RSELFRARTV GVGAYDTDTA LTWGTTGPGL RATGCDWDLR
KLRPYSGYEQ FDFEVPLGQR GDIFDRTRVR ADEMRESLKI IRQCLENMPE GPVKADHPLT
TPPPRGAMQK DIETLIAHFL QSSWGTVVPA GEATGQIEGH RGLTQYAIVS DGGTQSYRTR
IRTPSFAHLQ MIPKIVPGMT VADLVAHIAS IDFVMSDVDR
