ID A0A160FEG0_9BACI Unreviewed; 366 AA.
AC A0A160FEG0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:ANB65302.1};
GN ORFNames=GFC29_2604 {ECO:0000313|EMBL:ANB65302.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB65302.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB65302.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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; CP015436; ANB65302.1; -; Genomic_DNA.
DR RefSeq; WP_044741558.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160FEG0; -.
DR KEGG; anl:GFC29_2604; -.
DR PATRIC; fig|1490057.3.peg.2937; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000076753; 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:ANB65302.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000076753};
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; 41957 MW; 82258045F786D9DE CRC64;
MLRTEEMLLN VGPQHPSTHG VFRLVLKIDG EIIQEATPVI GYLHRGTEKL AENLQYTQII
PYTDRMDYLS AMTNNYVICH AVETMMGMKV PDRAEYLRVL AMELGRIASH LVWWGTYLLD
IGAISPFLYA FREREMIINL LNELSGARLT FNYMRVGGVK WDAPDGWIEK VKEFVPYMRK
QLAGYHELVT GNEIFRHRVM GVGRYTKEEA LSYSLSGANL RCTGVKWDLR KNEPYSIYDR
FDFDIPVRED GDCFARYECR LAEIEESLKI IEQACEQFPE KGEIMAKVPR IIKAPPGEAF
VRIESPRGEI GCYIASDGKK EPYRLKFRRP SFYNLQILPK LLKGENIANL IAILGAIDIV
LGEVDG
//
