ID A0A2K9L9F2_9RHOO Unreviewed; 417 AA.
AC A0A2K9L9F2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=B4966_04750 {ECO:0000313|EMBL:AUL99555.1};
OS Rhodocyclaceae bacterium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae.
OX NCBI_TaxID=1898103 {ECO:0000313|EMBL:AUL99555.1, ECO:0000313|Proteomes:UP000235024};
RN [1] {ECO:0000313|EMBL:AUL99555.1, ECO:0000313|Proteomes:UP000235024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thauera-like {ECO:0000313|EMBL:AUL99555.1,
RC ECO:0000313|Proteomes:UP000235024};
RA Umu S.U., Elley S., Stott M., Poole A.M.;
RT "A full genome of an Rhodocyclaceae isolate from Taupo Volcanic zone.";
RL Submitted (MAR-2017) 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
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|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC ECO:0000256|RuleBase:RU003685}.
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DR EMBL; CP020026; AUL99555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9L9F2; -.
DR KEGG; rbh:B4966_04750; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000235024; 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 Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000235024};
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};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 120..417
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 417 AA; 47953 MW; 96159FE3D609D1E1 CRC64;
MAEIRNYTIN FGPQHPSAHG VLRLVLELDG EVVERADPHI GLLHRGTEKL AETRTWVQSV
PYMDRLDYVS MMCNEHAYCM AIERLLGVQV PLRAQYIRVM FDEITRILNH LLNIGTHALD
IGAMTMVLYT FREREDLMDA YEAVSGARMH AAYYRPGGVY RDLPDRMPQY QVSRFKNEKT
VRELNAARQG SLLDFLEDFT ERFPRYCDEY ETLLTDNRIW KQRTVGIGVV SPEQALAWGF
SGPMLRGSGI AWDLRKKQPY EVYDQIDFDV PVGKNGDCYD RYLCRMEEMR QSNRIIRQCI
DWLRKNPGPV ITDNYKVAPP PREKMKTNME ELIHHFKLFT EGMHVPAGEV YAAVEHPKGE
FGVYAVSDGA NKPYRLKLRA PGFAHLAAMD EIARGHMIAD VVAIIGTMDI VFGEIDR
//
