ID A0A411YGJ3_9ACTN Unreviewed; 456 AA.
AC A0A411YGJ3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN Name=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
GN ORFNames=ER308_12830 {ECO:0000313|EMBL:QBI20360.1};
OS Egibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Nitriliruptoria; Egibacterales; Egibacteraceae;
OC Egibacter.
OX NCBI_TaxID=1670831 {ECO:0000313|EMBL:QBI20360.1, ECO:0000313|Proteomes:UP000291469};
RN [1] {ECO:0000313|EMBL:QBI20360.1, ECO:0000313|Proteomes:UP000291469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 80759 {ECO:0000313|EMBL:QBI20360.1,
RC ECO:0000313|Proteomes:UP000291469};
RA Chen D.-D., Tian Y., Jiao J.-Y., Zhang X.-T., Zhang Y.-G., Zhang Y.,
RA Xiao M., Shu W.-S., Li W.-J.;
RT "Egibacter rhizosphaerae EGI 80759T.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC ECO:0000256|RuleBase:RU003685}.
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DR EMBL; CP036402; QBI20360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411YGJ3; -.
DR KEGG; erz:ER308_12830; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000291469; 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 {ECO:0000256|HAMAP-Rule:MF_01358};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW Oxidoreductase {ECO:0000313|EMBL:QBI20360.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000291469};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01358};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 171..456
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..32
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 456 AA; 50306 MW; 73076E0876D48308 CRC64;
MTDTHGESGP DRTREGPVWQ GEEQPGSLAR TGESDYLVVG GEWQDLPEAV EDDTMVINMG
PQHPSTHGVL RLVLTLDGET VLSNDPVIGY LHTGIEKNTE YRPWVQGVTF VTRMDYLSPL
FNELGYCLAT ERILGIEEEV PERAQAIRVI LTELNRVSSH MVWLATGGME LGSTTAMIFG
FRERESVLDI FEHVTGLRMN HGFIRPGGLA NDVPDTFDAR VRQVISELRQ RIDEIEDLLT
KNPIWIERNK GVGIMDAETC LDYGATGPVL RSAGIAHDLR KAQPYCGIEQ YDFEVPITDT
ADSYGRYLIR VQEVRESLSI VEQALDRLPG GRVMVDDDKI AWPAQLGLGP DGLGNTEEYI
SKIMGQSMEA LIHHFKIVTE GFTAPPGQAY AAVESPRGEL GYHITSNGTN KPYRVRVRDP
SFIHIGALDP LSRGLGVADI IVAVASVDPV MGGVDR
//
