NUOD2_STRGG
ID NUOD2_STRGG Reviewed; 394 AA.
AC B1VSH7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=SGR_4102;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(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 a
CC menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01358};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358};
CC 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; AP009493; BAG20931.1; -; Genomic_DNA.
DR AlphaFoldDB; B1VSH7; -.
DR SMR; B1VSH7; -.
DR STRING; 455632.SGR_4102; -.
DR EnsemblBacteria; BAG20931; BAG20931; SGR_4102.
DR KEGG; sgr:SGR_4102; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_11; -.
DR OMA; GGRMHYM; -.
DR Proteomes; UP000001685; 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 PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Translocase; Transport.
FT CHAIN 1..394
FT /note="NADH-quinone oxidoreductase subunit D 2"
FT /id="PRO_0000357942"
SQ SEQUENCE 394 AA; 43554 MW; 6D647CBF2B604DF4 CRC64;
MTPAADPGQG ILSRMTETTI GIGGAAESTD MVLNIGPQHP STHGVLRLRI VLDGERVQHA
EPVIGYMHRG AEKLFEARDY RQIIMLANRH DWLSAFSNEL GVVMAVERML GMEVPERAVW
TRTLLAELNR VLNHLMFLGS YPLELGGITP VFHAFREREE LQAVMEEVSG GRMHYMFNRV
GGLKEDVPAG WAGRVRDAVA SVRSRMDVYE NLVLGNEIFR GRTRDVGVLS AAAVHAYGVS
GPIARASGVD FDLRRDEPYL AYGELRDTLK VVTRTEGDCL ARFECLLEQT LNSLDLADAC
LDRMAHLAPG PINQRLPKVL KAPEGHTYAW TENPLGVNGY YLVSKGEKTP YRLKLRSASF
NNIQALTELL PGTLVADMVA ILGSLFFVVG DIDK