GenomeNet

Database: UniProt
Entry: A0A0E3ZCB7_9BACT
LinkDB: A0A0E3ZCB7_9BACT
Original site: A0A0E3ZCB7_9BACT 
ID   A0A0E3ZCB7_9BACT        Unreviewed;       414 AA.
AC   A0A0E3ZCB7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=PKOR_03615 {ECO:0000313|EMBL:AKD02379.1};
OS   Pontibacter korlensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD02379.1, ECO:0000313|Proteomes:UP000033109};
RN   [1] {ECO:0000313|EMBL:AKD02379.1, ECO:0000313|Proteomes:UP000033109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14-1T {ECO:0000313|EMBL:AKD02379.1,
RC   ECO:0000313|Proteomes:UP000033109};
RX   PubMed=26057562; DOI=10.1038/srep10929;
RA   Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA   Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT   "Unraveling adaptation of Pontibacter korlensis to radiation and
RT   infertility in desert through complete genome and comparative
RT   transcriptomic analysis.";
RL   Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD02379.1; -; Genomic_DNA.
DR   RefSeq; WP_046309170.1; NZ_CP009621.1.
DR   AlphaFoldDB; A0A0E3ZCB7; -.
DR   STRING; 400092.PKOR_03615; -.
DR   KEGG; pko:PKOR_03615; -.
DR   PATRIC; fig|400092.3.peg.816; -.
DR   HOGENOM; CLU_015134_1_2_10; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000033109; 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   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:AKD02379.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033109};
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}.
FT   DOMAIN          144..413
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   414 AA;  47156 MW;  852F838B1065BF0F CRC64;
     MATENKTAEL TELEQFRKEH GLAIHEERQL TTLNLGPTHP ATHGIFQNIL QMDGEIIVDA
     VPTIGYIHRA FEKIAERRPF YQITPLTDRM NYCSAPINNM GYHMTVEKLL GITVPKRAQY
     IRVIMMELAR ISDHLICNSI LGVDSGAFTG FLYVMQEREH IYDIYEEVCG ARLTTNMGRI
     GGMERDLSPK ALHMIDEFLK RFPKVWAEFE KMMTRNRIFM DRTTGVGAIS AERALSYGFT
     GPNLRAAGVD YDVRVMNPYS SYEDFEFEIP VGSKGDTYDR FLVRNEEVWQ SLKIIEQAYK
     NLPEGSYHAD APHYYLPPKQ AVYTSMEALI YHFKIVMGET DAPVGEVYHS VEGGNGELGF
     YLISDGGRTP YRLHFRRPCF IYYQAYTEMI KGGQLADAIL TLSSLNVIAG ELDA
//
DBGET integrated database retrieval system