ID NUOD_NOCFA Reviewed; 453 AA.
AC Q5YWD0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
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=NFA_26640;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57511.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YWD0; -.
DR SMR; Q5YWD0; -.
DR STRING; 247156.NFA_26640; -.
DR KEGG; nfa:NFA_26640; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_11; -.
DR Proteomes; UP000006820; 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; Cytochrome-c3 Hydrogenase, chain B; 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 NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..453
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000357875"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50054 MW; D87AF6A4BFA0C200 CRC64;
MKDTETRPGR HRAPEPAHPE QPDTTGDTVV TVSGQDWDTV TETLGGAREE RIVVNMGPQH
PSTHGVLRLI LEIEGETVVE ARCGIGYLHT GIEKNLEYRT WMQGVTFVTR MDYLSPFYNE
TAYCLGVERL LGITEQIPER ASIVRVLLME LNRISSHLVC LATGGMELGA LTPMLFGFRE
RELILDVFET ITGLRMNHAY IRPGGLAQDL PDDGVAKVRE LLDLMPKRLR DMEHLLTQNP
IFKARTQDIG YLDLTGCMAL GITGPVLRSA GLPHDLRKSQ PYCGYETYEF DVPTTTGCDC
YGRYLIRVEE MKESLKIVEQ CLDRLRPGPV MIEDKKLAWP ADLKLGADGL GNSPAHIGRI
MGSSMEGLIH HFKLVTEGIR VPAGQVYVAV ESPRGELGVH MVSDGGTRPY RVHYRDPSFT
NLQAVAAMCE GGMVADVIAA VASIDPVMGG VDR
//
