ID A0A3G9JFW2_9BACL Unreviewed; 366 AA.
AC A0A3G9JFW2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-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 ECO:0000313|EMBL:BBH23863.1};
GN ORFNames=Back11_52080 {ECO:0000313|EMBL:BBH23863.1}, FHS14_002032
GN {ECO:0000313|EMBL:MBB3069045.1};
OS Paenibacillus baekrokdamisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1712516 {ECO:0000313|EMBL:BBH23863.1, ECO:0000313|Proteomes:UP000275368};
RN [1] {ECO:0000313|EMBL:BBH23863.1, ECO:0000313|Proteomes:UP000275368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33723 {ECO:0000313|EMBL:BBH23863.1,
RC ECO:0000313|Proteomes:UP000275368};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Lee J.S.;
RT "Complete genome sequence of Paenibacillus baekrokdamisoli strain KCTC
RT 33723.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3069045.1, ECO:0000313|Proteomes:UP000562277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8890 {ECO:0000313|EMBL:MBB3069045.1,
RC ECO:0000313|Proteomes:UP000562277};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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|HAMAP-Rule:MF_01358}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP019308; BBH23863.1; -; Genomic_DNA.
DR EMBL; JACHXC010000003; MBB3069045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9JFW2; -.
DR KEGG; pbk:Back11_52080; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000275368; Chromosome.
DR Proteomes; UP000562277; Unassembled WGS sequence.
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 Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000275368};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01358};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 120..291
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 292..365
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 366 AA; 41696 MW; 72D1378ADE5479C0 CRC64;
MIRTEELLLN VGPQHPSTHG VFRIVVKLDG EVITEATPVM GYLHRGTEKL AEDLNYTQII
PYTDRMDYVS AMTTNYVLCH AVETMMGLEV PIRAEFMRLI VMELQRVASH LVWWGTYLLD
IGAMSPFLFA FRDREIIIDL FNELCGARLT YNYMRVGGVK WDAPDGWIDK VRDFIPYMEK
KLDEYNDLVS GNEIFLARIK GVGKYDAQTA IEYGLSGANL RCTGVDWDLR KAEPYSLYSQ
FEFDVPLGRN GDCYDRYLIR LEEVRQSLRI LKQAVQQFPP AGDVMGKVPR VIRPPAGEVY
VRIESPRGEI GCHIVSKGKA EPYRLKFRRP SFVNLQILPK LLVGETMTNL ITILGGIDIV
VGEVDC
//
