ID A0A0R0E5V6_9GAMM Unreviewed; 435 AA.
AC A0A0R0E5V6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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=ABB34_07765 {ECO:0000313|EMBL:KRG85534.1};
OS Stenotrophomonas daejeonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG85534.1, ECO:0000313|Proteomes:UP000050940};
RN [1] {ECO:0000313|EMBL:KRG85534.1, ECO:0000313|Proteomes:UP000050940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG85534.1,
RC ECO:0000313|Proteomes:UP000050940};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG85534.1}.
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DR EMBL; LDJP01000043; KRG85534.1; -; Genomic_DNA.
DR RefSeq; WP_057640712.1; NZ_LDJP01000043.1.
DR AlphaFoldDB; A0A0R0E5V6; -.
DR STRING; 659018.ABB34_07765; -.
DR PATRIC; fig|659018.3.peg.1490; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000050940; 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; 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 Oxidoreductase {ECO:0000313|EMBL:KRG85534.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000050940};
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 138..435
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 435 AA; 49443 MW; 2318F59CFB637DA5 CRC64;
MNEFQQAHEA FASNPAEARQ EIRNYTMNFG PQHPAAHGVL RLILEMDGET IVRADPHVGL
LHRATEKLAE SKPFNQSIGY MDRLDYCSMM CNEHAYVRAI ETLMGIEAPE RAQYIRTLFD
EVTRILNHLM WLGSNALDLG AMAVMLYAFR EREELMDCYE AVSGARMHAT YYRPGGVYRD
LPDAMPKYKE SRWHKGGALK RLNAAREGSL LDFLENFTNE FPKRVDEYET LLTDNRIWKQ
RTVGIGVVTP EHALAWGMTG VMLRGSGIEW DLRKKQPYAK YDAVDFDIPL GKEGDCYDRY
LVRVAEMRES NRIVKQCVQW LKANPGPVMV RNFKVAPPKR AEMKEDMEAL IHHFKLFSEG
YCVPAGETYA AVEAPKGEFG CYLVSDGANK PFRAHLRAPG FAHLSSIDSV VRGHMLADVV
AMVGTYDLVF GEVDR
//
