NQO11_PARDE
ID NQO11_PARDE Reviewed; 101 AA.
AC P29923;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=NADH-quinone oxidoreductase subunit 11;
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NADH dehydrogenase I, subunit 11;
DE AltName: Full=NDH-1, subunit 11;
GN Name=nqo11 {ECO:0000303|PubMed:8422400};
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=8422400; DOI=10.1021/bi00054a030;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "DNA sequencing of the seven remaining structural genes of the gene cluster
RT encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus
RT denitrificans.";
RL Biochemistry 32:968-981(1993).
RN [2]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11914084; DOI=10.1021/bi025525d;
RA Kao M.-C., Di Bernardo S., Matsuno-Yagi A., Yagi T.;
RT "Characterization of the membrane domain Nqo11 subunit of the proton-
RT translocating NADH-quinone oxidoreductase of Paracoccus denitrificans.";
RL Biochemistry 41:4377-4384(2002).
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.
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:0000255|HAMAP-Rule:MF_01456};
CC -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, Nqo1 to
CC Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01456, ECO:0000269|PubMed:11914084}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01456, ECO:0000269|PubMed:11914084}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4L family.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR EMBL; L02354; AAA25597.1; -; Genomic_DNA.
DR PIR; G45456; G45456.
DR RefSeq; WP_010392916.1; NZ_PPGA01000003.1.
DR AlphaFoldDB; P29923; -.
DR SMR; P29923; -.
DR TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR OMA; NFVAFSY; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_01456; NDH1_NuoK; 1.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..101
FT /note="NADH-quinone oxidoreductase subunit 11"
FT /id="PRO_0000118522"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11914084"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 25..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11914084"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 51..64
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11914084"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 86..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11914084"
SQ SEQUENCE 101 AA; 10856 MW; A8061FD86A8B9AB8 CRC64;
MIGLTHYLVV GAILFVTGIF GIFVNRKNVI VILMSIELML LAVNINFVAF STHLGDLAGQ
VFTMFVLTVA AAEAAIGLAI LVVFFRNRGT IAVEDVNVMK G
