NUOCD_ACICJ
ID NUOCD_ACICJ Reviewed; 592 AA.
AC A5FXJ8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Acry_1118;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ30330.1; -; Genomic_DNA.
DR RefSeq; WP_011942003.1; NC_009484.1.
DR AlphaFoldDB; A5FXJ8; -.
DR SMR; A5FXJ8; -.
DR STRING; 349163.Acry_1118; -.
DR PRIDE; A5FXJ8; -.
DR EnsemblBacteria; ABQ30330; ABQ30330; Acry_1118.
DR KEGG; acr:Acry_1118; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_3_2_5; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000000245; Chromosome.
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_01357; NDH1_NuoC; 1.
DR HAMAP; MF_01359; NDH1_NuoCD_1; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR010218; NADH_DH_suC.
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; TIGR01961; NuoC_fam; 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..592
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000358605"
FT REGION 1..183
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT REGION 207..592
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ SEQUENCE 592 AA; 68008 MW; 9999FE225681BBA8 CRC64;
MLTEFNSIPA TEAEQGIVSD LVRTLGPISF TLQQTADRIP TIWIDRDIVH AVLRHLRDGA
TRRFQMLYDL TAIDERQRVH RDGLPKSDFT LVYHLVSFER NDDVRVKVPL AEGALEVQSI
ADIWPNANWY EREVWDMFGI GFAGHPTLFR ILTPPTWTGH PLRKDYIARA TEMGPYILTE
EKERAEQEAL RFNPEAWGMK RHSENSDFMF LNLGPNHPSV HGVFRIILQL EGEEIVDAVP
EIGFHHRGAE KMAERQSWHT YIPYTDRIDY LGGVMNNFPY VMAVERLAGI EVPSRAQMIR
IMLAELFRIA SHLVFYGTMS QDVGQLSPVF YMFSDRERVF QIIEAICGFR MHPAWFRIGG
VAADLPQGWD RMIRDYLGYQ SKRLDEYDKL VMRNRLFKAR TIGVGAYTLE EALDWGVTGP
GLRACGLGWD YRRQRPYSGY DQLEFDIPIC HNGDCYDRVV VHIEEIRQSL RIIRQCLDNM
PPGPYKSDHR LTTPPLKERT MQDIETLITH FLNVSWGPVL PPGEAMVSIE ATKGINGYYL
VADGDTVSYR TRIRTPSFPH LQMIPLISRG AYVADLIAII GSIDFVMADV DR
