NUOD_HELAH
ID NUOD_HELAH Reviewed; 409 AA.
AC Q17Z55;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Hac_0221;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99071.1; -; Genomic_DNA.
DR RefSeq; WP_011577187.1; NC_008229.1.
DR AlphaFoldDB; Q17Z55; -.
DR SMR; Q17Z55; -.
DR STRING; 382638.Hac_0221; -.
DR PRIDE; Q17Z55; -.
DR EnsemblBacteria; CAJ99071; CAJ99071; Hac_0221.
DR KEGG; hac:Hac_0221; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_7; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR BioCyc; HACI382638:HAC_RS00990-MON; -.
DR Proteomes; UP000000775; 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; 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.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transport; Ubiquinone.
FT CHAIN 1..409
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000371875"
SQ SEQUENCE 409 AA; 46690 MW; ED825498BDCB30D2 CRC64;
MAQNFTKLNP QFENIIFEHD DNQMVLNFGP QHPSSHGQLR LILELEGERI IKATPEIGYL
HRGCEKLGEN MTYNEYMPTT DRLDYTSSAS NNYAYAHAVE TLLNLEIPRR AQVIRTILLE
LNRMISHIFF ISVHALDVGA MSVFLYAFKT REHGLDLMED YCGARLTHNA IRIGGVPLDL
PPNWLEGLKK FLGEMRECKK LIQGLLDKNR IWRMRLENVG VVTPKMAQSW GMSGIMLRGT
GIAYDIRKEE PYELYRELDF DVPVGNYGDS YDRYCLYMLE IDESIRIIEQ LIPMYAKTDT
PIMAQNPHYI SAPKEDIMTQ NYALMQHFVL VAQGMRPPIG EVYAPTESPK GELGFFIHSE
GESYPHRLKI RAPSFYHIGS LGDILVGQYL ADAVTVIGST NAVFGEVDR