ID   A0A249SMS0_9MOLU        Unreviewed;       452 AA.
AC   A0A249SMS0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:ASZ08801.1};
GN   ORFNames=CK556_00265 {ECO:0000313|EMBL:ASZ08801.1};
OS   Mesoplasma chauliocola.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=216427 {ECO:0000313|EMBL:ASZ08801.1, ECO:0000313|Proteomes:UP000232229};
RN   [1] {ECO:0000313|EMBL:ASZ08801.1, ECO:0000313|Proteomes:UP000232229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHPA-2 {ECO:0000313|EMBL:ASZ08801.1,
RC   ECO:0000313|Proteomes:UP000232229};
RA   Knight T.F.Jr., Citino T.;
RT   "Complete Genome Sequence of Mesoplasma chauliocola.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR   EMBL; CP023173; ASZ08801.1; -; Genomic_DNA.
DR   RefSeq; WP_027875814.1; NZ_CP023173.1.
DR   AlphaFoldDB; A0A249SMS0; -.
DR   STRING; 1336232.GCA_000518825_00678; -.
DR   KEGG; mchc:CK556_00265; -.
DR   Proteomes; UP000232229; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   PRINTS; PR00411; PNDRDTASEI.
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;
FT   DOMAIN          1..307
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          334..430
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   452 AA;  49712 MW;  941235E094405A15 CRC64;
     MKVIVLGTNH AGTTAVRTLK RLNPEIEVVT YDRNDVISFL GCGIALWVKG EVKDPNGLFY
     ATPEILESEG IVVKMKHEWV SIDADKKTVL IKNLETGETF EDSYDKVIVA TGTWPLLPPI
     PGLDLNGVQI CKNYDHAKVI QKANLDDSIK KVTVVGAGYI GVELVDAFVA HGKEVTLVDF
     ADRIMPVYYD AEFTKHVEDR MEKAGVKLAL SQGVKEFKGT NGKVTHVVTD KEEIATDYVI
     FSVGVVAQTK PLEGVVELSD RKAVITNDYC QSSNPDIYAI GDCSTVFNKA LNMEMPIQLA
     TTAVRTGILA AANIVNGNKL PSPGFTGANG IEVFGFKMAS AGVSETSAKK MGLDYEAILL
     SDSDRPEFMS TYKEAWIKLV WDKKSRKIIG AQVASENNHT EIMYMLSLGI QKELTIDELP
     LVDIFFLPHF NKPYNFVTLA GLEVLGLNYF KK
//