NUOD2_SOLUE
ID NUOD2_SOLUE Reviewed; 370 AA.
AC Q01UN9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=NADH-quinone oxidoreductase subunit D 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit D 2 {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=nuoD2 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=Acid_5684;
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC Candidatus Solibacter.
OX NCBI_TaxID=234267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin6076;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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}.
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DR EMBL; CP000473; ABJ86631.1; -; Genomic_DNA.
DR RefSeq; WP_011687366.1; NC_008536.1.
DR AlphaFoldDB; Q01UN9; -.
DR SMR; Q01UN9; -.
DR STRING; 234267.Acid_5684; -.
DR EnsemblBacteria; ABJ86631; ABJ86631; Acid_5684.
DR KEGG; sus:Acid_5684; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_0; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
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; 2.
DR SUPFAM; SSF56762; SSF56762; 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..370
FT /note="NADH-quinone oxidoreductase subunit D 2"
FT /id="PRO_0000371925"
SQ SEQUENCE 370 AA; 41613 MW; 1C75AD34CE223D4F CRC64;
MPDSTFLDST ELVLNMGPQH PSTHGVLRVI LKLDGEKVLG TDCIIGYLHR GVEKIAENRT
YAQFNPYVDR MDYVAAVSNG LGYCLAIEKL LNVEAPPRAQ CIRVILTELN RIASHLLWLG
THALDIGAIT PVFYCLRERE EALKIFEKYC GARLTTHAFR IGGLLYETYD GFEQEIRDFC
KMFIPKVDEY EELLTNNRIW VGRLKDVGIL SADECKEFGV TGPVLRAAGV KWDLRKAQPY
SGYEKYDFEI PTRVNGDTYD RYIVRMEEMR QSVRIMQQAV DGIPEGPIMG KVGKVIKPPI
GEAYVSIEAP KGELGYYAVS DGSTQPYRIR VRPPSFVNLQ ALDRMIRGGL IADVVAVIGT
LDIVLGEIDR