ID A0A2U8E222_9BACT Unreviewed; 416 AA.
AC A0A2U8E222;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CKA38_04270 {ECO:0000313|EMBL:AWI08572.1};
OS Ereboglobus luteus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Ereboglobus.
OX NCBI_TaxID=1796921 {ECO:0000313|EMBL:AWI08572.1, ECO:0000313|Proteomes:UP000244896};
RN [1] {ECO:0000313|EMBL:AWI08572.1, ECO:0000313|Proteomes:UP000244896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ho45 {ECO:0000313|EMBL:AWI08572.1,
RC ECO:0000313|Proteomes:UP000244896};
RX PubMed=29295750; DOI=10.1016/j.syapm.2017.10.005;
RA Tegtmeier D., Belitz A., Radek R., Heimerl T., Brune A.;
RT "Ereboglobus luteus gen. nov. sp. nov. from cockroach guts, and new
RT insights into the oxygen relationship of the genera Opitutus and
RT Didymococcus (Verrucomicrobia: Opitutaceae).";
RL Syst. Appl. Microbiol. 41:101-112(2018).
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: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|HAMAP-Rule:MF_01358}.
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DR EMBL; CP023004; AWI08572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8E222; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000244896; 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; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
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; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 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|HAMAP-Rule:MF_01358};
KW Oxidoreductase {ECO:0000313|EMBL:AWI08572.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000244896};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01358};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01358};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 171..337
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 338..416
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46331 MW; 4AA353921B762018 CRC64;
MNNASTSSAP TTANATEAEA PVSPFPLHSS PFGPSSASGA TVRAVNDEFH GDLLEISLGP
HHPSTHGVFR MNAALDGEIV TKLKPVFGYL HRNHEKLGET NSYLANVPYT DRLDYLASLT
NNWAYVHAVE KLAGITPTER CEYLRVILGE LGRIINHVCL VGFLLNDLGT SFTPLLYSLR
ERERMLDLLE ELTGARMMYN FFRFGGLRTD VSADWLARLK HYLEGLFARY LDEQDALLTG
NEILLARTQG TGILKPDLAI NAGFTGPGLR ASGVDYDIRK VDKYSIYDRF DFRVPLGEHG
DTYDRFMMRM LEMRESVKII LQAMRDLPDG PVNDPKAKSR GLRPKAGEAY GRIECPKGEL
GFYLISDGTP NPYRYRVRPP SFINLTILED LCLGQTLADT IIILGSIDIV LGEVDR
//