ID A0A1A5XK68_9BACL Unreviewed; 382 AA.
AC A0A1A5XK68;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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 ORFNames=A6764_02780 {ECO:0000313|EMBL:UYZ13924.1}, A6764_12020
GN {ECO:0000313|EMBL:OBR53550.1};
OS Brevibacillus sp. WF146.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR53550.1};
RN [1] {ECO:0000313|EMBL:OBR53550.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF146 {ECO:0000313|EMBL:OBR53550.1};
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.
RN [2] {ECO:0000313|EMBL:UYZ13924.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WF146 {ECO:0000313|EMBL:UYZ13924.1};
RA Tang B., Tang X.-F., Zhu F., Li Y.;
RT "Complete genome sequence of Brevibacillus thermoruber WF146.";
RL Submitted (OCT-2022) 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}.
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DR EMBL; LXGJ01000189; OBR53550.1; -; Genomic_DNA.
DR EMBL; CP109943; UYZ13924.1; -; Genomic_DNA.
DR RefSeq; WP_065067429.1; NZ_LXGJ01000189.1.
DR AlphaFoldDB; A0A1A5XK68; -.
DR Proteomes; UP000093585; 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:UYZ13924.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000093585};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01358};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 136..306
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 308..381
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 382 AA; 43592 MW; B04B37681738B5C6 CRC64;
MNRDILLTNA TTSPESGIRT EEMLLNVGPQ HPSTHGVLRL VVKIDGETIK EATPVMGYLH
RGTEKLAENL TYTQIIPYTD RMDYVSAMTN NYVLCHAVET MMGVEVPERA QFLRLIAMEL
NRVASHLVWW GTYLLDIGAM GPFLYAFRDR ESILDLFNEL CGARMTFNYM RIGGVKWDAP
PGWIDKVKEF VQYMKKELNN YHKLVTGNEI FINRLRGIGK FDQKTALDYS LSGVMLRSTG
VKWDLRKDEP YCIYDRFEFD VPTATEGDCL ARYHLRMAEI EQSLRILEQA LDQFPTEGEV
MGKVPRVIRP PAGEAYVRIE SPRGEIGCYI ASTGKDKPWR LKFRRPSFHN LQILPKLLEG
ENIANMVAIL GSIDIVLGEV DC
//
