GenomeNet

Database: UniProt
Entry: G7WEA6_DESOD
LinkDB: G7WEA6_DESOD
Original site: G7WEA6_DESOD 
ID   G7WEA6_DESOD            Unreviewed;       367 AA.
AC   G7WEA6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=Desor_4678 {ECO:0000313|EMBL:AET70082.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET70082.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET70082.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC       ECO:0000256|RuleBase:RU003685}.
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; CP003108; AET70082.1; -; Genomic_DNA.
DR   RefSeq; WP_014186889.1; NC_016584.1.
DR   AlphaFoldDB; G7WEA6; -.
DR   STRING; 768706.Desor_4678; -.
DR   KEGG; dor:Desor_4678; -.
DR   PATRIC; fig|768706.3.peg.4758; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_9; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000006346; 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   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.
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:UP000006346};
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:0000313|EMBL:AET70082.1}.
FT   DOMAIN          122..295
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          293..367
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   367 AA;  41369 MW;  FDAEB007104A5F4A CRC64;
     MSIGKTEELV LNMGPQHPSM HGLFRMVVHL EGETVTHIDP KLGYLHRGME KLAESRTYTQ
     FIPYTDRLDY LASPHNNLAY VQTVEKLMGV EIPERGEYLR VIFAELARIA SHQVMIASTA
     LDLAGWTAWS YAFRDRERIC DMYEMTAGSR LTVNIMRIGG ISAEPPEEFW PALQSFLDDS
     PEMIEEYYGI FFGNEIALGR LKNVGILTKE MAENLSVTGP VLRASGVDYD VRKAEPYGIY
     DRFDFKVPVR TGCDSYDRTI LRLDEIVESI KIIKQAVRDI PGGPIMAKVP KVIKPPAGEV
     YHRVENPKGE LGFYIVSNGT TKPERLRIRP GTFINLQMLP IVAKGWKIQD VVAIFATLDA
     VLGEVDK
//
DBGET integrated database retrieval system