NAOX_MYCPN
ID NAOX_MYCPN Reviewed; 479 AA.
AC P75389;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable NADH oxidase;
DE Short=NOXase;
DE EC=7.1.1.2;
GN Name=nox; OrderedLocusNames=MPN_394; ORFNames=MP444;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC water. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U00089; AAB96092.1; -; Genomic_DNA.
DR PIR; S73770; S73770.
DR RefSeq; NP_110082.1; NC_000912.1.
DR RefSeq; WP_010874750.1; NC_000912.1.
DR AlphaFoldDB; P75389; -.
DR SMR; P75389; -.
DR IntAct; P75389; 2.
DR STRING; 272634.MPN_394; -.
DR EnsemblBacteria; AAB96092; AAB96092; MPN_394.
DR GeneID; 66608947; -.
DR KEGG; mpn:MPN_394; -.
DR PATRIC; fig|272634.6.peg.425; -.
DR HOGENOM; CLU_003291_1_0_14; -.
DR OMA; ACGIPYW; -.
DR BioCyc; MPNE272634:G1GJ3-626-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Redox-active center;
KW Reference proteome; Translocase.
FT CHAIN 1..479
FT /note="Probable NADH oxidase"
FT /id="PRO_0000184703"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 43
FT /note="Redox-active"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 111..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 170..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 295..305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 52875 MW; 66B86EA3BA8E53F1 CRC64;
MKKVIVIGVN HAGTSFIRTL LSKSKDFQVN AYDRNTNISF LGCGIALAVS GVVKNTEDLF
YSTPEELKAM GANVFMAHDV VGLDLDKKQV IVKDLATGKE TVDHYDQLVV ASGAWPICMN
VENEVTHTQL QFNHTDKYCG NIKNLISCKL YQHALTLIDS FRHDKSIKSV AIVGSGYIGL
ELAEAAWQCG KQVTVIDMLD KPAGNNFDEE FTNELEKAMK KAGINLMMGS AVKGFIVDAD
KNVVKGVETD KGRVDADLVI QSIGFRPNTQ FVPKDRQFEF NRNGSIKVNE YLQALNHENV
YVIGGAAAIY DAASEQYENI DLATNAVKSG LVAAMHMIGS KAVKLESIVG TNALHVFGLN
LAATGLTEKR AKMNGFDVGV SIVDDNDRPE FMGTFDKVRF KLIYDKKTLR LLGAQLLSWN
TNHSEIIFYI ALAVQKKMLI SELGLVDVYF LPHYNKPFNF VLAAVLQALG FSYYTPKNK
