NQO2_PARDE
ID NQO2_PARDE Reviewed; 239 AA.
AC P29914;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NADH-quinone oxidoreductase chain 2;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I, chain 2;
DE AltName: Full=NDH-1, chain 2;
GN Name=nqo2;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=1909571; DOI=10.1021/bi00099a027;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "Characterization of the 25-kilodalton subunit of the energy-transducing
RT NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence
RT similarity to the 24-kilodalton subunit of the flavoprotein fraction of
RT mammalian complex I.";
RL Biochemistry 30:8678-8684(1991).
RN [2]
RP PROBABLE 2FE-2S CLUSTER, AND MUTAGENESIS OF CYS-61; HIS-92; CYS-96;
RP CYS-101; CYS-104; CYS-113; CYS-137 AND CYS-141.
RX PubMed=7957917; DOI=10.1016/0014-5793(94)01107-9;
RA Yano T., Sled V.D., Ohnishi T., Yagi T.;
RT "Identification of amino acid residues associated with the [2Fe-2S] cluster
RT of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone
RT oxidoreductase of Paracoccus denitrificans.";
RL FEBS Lett. 354:160-164(1994).
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000305|PubMed:7957917};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305|PubMed:7957917};
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; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M74171; AAA25588.1; -; Genomic_DNA.
DR PIR; A40296; A40296.
DR RefSeq; WP_011748532.1; NZ_PPGA01000003.1.
DR AlphaFoldDB; P29914; -.
DR SMR; P29914; -.
DR TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR OMA; VGKFHVQ; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Quinone; Translocase;
KW Ubiquinone.
FT CHAIN 1..239
FT /note="NADH-quinone oxidoreductase chain 2"
FT /id="PRO_0000118685"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:7957917"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:7957917"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:7957917"
FT BINDING 141
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:7957917"
FT MUTAGEN 61
FT /note="C->S: No change in UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 92
FT /note="H->A: No change in UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 96
FT /note="C->A,S: Alters UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 101
FT /note="C->A,S: Alters UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 104
FT /note="C->S: No change in UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 113
FT /note="C->S: No change in UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 137
FT /note="C->A,S: Alters UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
FT MUTAGEN 141
FT /note="C->A,S: Alters UV-visible and EPR spectra."
FT /evidence="ECO:0000269|PubMed:7957917"
SQ SEQUENCE 239 AA; 26122 MW; 6BF734257D670F41 CRC64;
MLRRLSPIQP DSFEFTPANL EWARAQMTKY PEGRQQSAII PVLWRAQEQE GWLSRPAIEY
CADLLGMPYI RALEVATFYF MFQLQPVGSV AHIQICGTTT CMICGAEDLI RVCKEKIAPE
PHALSADGRF SWEEVECLGA CTNAPMAQIG KDFYEDLTVE KLAALIDRFA AGEVPVPGPQ
NGRFSAEALG GPTALADLKG GEAHNASVAR ALRLGDSIKR IDGTEVPITT PWLATQNGV
