NUOD_RICRO
ID NUOD_RICRO Reviewed; 391 AA.
AC B0BX71;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
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=RrIowa_0576;
OS Rickettsia rickettsii (strain Iowa).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=452659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa;
RX PubMed=18025092; DOI=10.1128/iai.00952-07;
RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA Hackstadt T.;
RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT avirulent Rickettsia rickettsii Iowa.";
RL Infect. Immun. 76:542-550(2008).
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_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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABY72447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000766; ABY72447.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014362466.1; NC_010263.3.
DR AlphaFoldDB; B0BX71; -.
DR SMR; B0BX71; -.
DR STRING; 452659.RrIowa_0576; -.
DR EnsemblBacteria; ABY72447; ABY72447; RrIowa_0576.
DR GeneID; 45539064; -.
DR KEGG; rrj:RrIowa_0576; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_5; -.
DR Proteomes; UP000000796; 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; 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; PF00346; Complex1_49kDa; 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; NAD; Quinone; Translocase;
KW Transport; Ubiquinone.
FT CHAIN 1..391
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000357914"
SQ SEQUENCE 391 AA; 44683 MW; 83DF3F93D6B16876 CRC64;
MTNNTKTITL NLGPQHPATH GVLRLILEMD GEVVNNADPH IGLLHRGTEK LIEHKTYLQA
IPYFDRLDYV SPMCQEHAFA LAVESLLECE VPRRAQFIRV LFSELTRILN HTLNIGSQAL
DIGATTPLLW LFEEREKIME FYEHVSGSRM HSNYFRPGGV VADLPEGLLE DIDKFIEQFP
PKLHDIESLL NENRLWKQRL VDIGVVSQKE AMDWGFSGPM LRGSGIAWDL RKSNPYDVYD
EMDFKVPIGK NGDCYDRYFV RMLEMYESIK IIKQCIEKMP KGAIKTDDPK LTPPTRAKMK
ESMEAMIHHF KLYTEGYDVP AGETYKAVEA PKGEFGVYLY SRGGNRPYRC RIKAPGFAHL
QGLDFMSQGH LMADVITIIA TLDIVFGEID R