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 27-MAR-2024, entry version 117. DE RecName: Full=NADH oxidase; DE Short=NOXase; DE EC=1.6.3.4 {ECO:0000250|UniProtKB:A2RIB7}; GN Name=nox; OrderedLocusNames=MPN_394; ORFNames=MP444; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; 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: [NADH oxidase]: CC Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.4; CC Evidence={ECO:0000250|UniProtKB:A2RIB7}; 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}. 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; U00089; AAB96092.1; -; Genomic_DNA. DR PIR; S73770; S73770. DR RefSeq; NP_110082.1; NC_000912.1. DR RefSeq; WP_010874750.1; NZ_OU342337.1. 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 OrthoDB; 9792592at2; -. DR BioCyc; MPNE272634:G1GJ3-626-MONOMER; -. 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 Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1. DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. PE 3: Inferred from homology; KW FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Redox-active center; KW Reference proteome. FT CHAIN 1..479 FT /note="NADH oxidase" FT /id="PRO_0000184703" FT ACT_SITE 11 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P37062" 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 33 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 43 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 80 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 111..114 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 170..185 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P37062" FT BINDING 264 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P37062" FT BINDING 295..305 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 323 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 324 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT BINDING 353 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P37062" FT BINDING 450 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" FT MOD_RES 43 FT /note="Cysteine sulfinic acid (-SO2H)" FT /evidence="ECO:0000250|UniProtKB:Q5XC60" 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 //