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Database: UniProt
Entry: N9TSC5_9MOLU
LinkDB: N9TSC5_9MOLU
Original site: N9TSC5_9MOLU 
ID   N9TSC5_9MOLU            Unreviewed;       454 AA.
AC   N9TSC5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:ENY68990.1};
GN   Name=nox {ECO:0000313|EMBL:ENY68990.1};
GN   ORFNames=MBVG_6680 {ECO:0000313|EMBL:ENY68990.1};
OS   Mycoplasmopsis bovigenitalium 51080.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=1188235 {ECO:0000313|EMBL:ENY68990.1, ECO:0000313|Proteomes:UP000013220};
RN   [1] {ECO:0000313|EMBL:ENY68990.1, ECO:0000313|Proteomes:UP000013220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=51080 {ECO:0000313|EMBL:ENY68990.1,
RC   ECO:0000313|Proteomes:UP000013220};
RX   PubMed=23766408;
RA   Manso-Silvan L., Tardy F., Baranowski E., Barre A., Blanchard A.,
RA   Breton M., Couture C., Citti C., Dordet-Frisoni E., Dupuy V., Gaurivaud P.,
RA   Jacob D., Lemaitre C., Nikolski M., Nouvel L.X., Poumarat F., Thebault P.,
RA   Theil S., Thiaucourt F., Sirand-Pugnet P.;
RT   "Draft Genome Sequences of Mycoplasma alkalescens, Mycoplasma arginini, and
RT   Mycoplasma bovigenitalium, Three Species with Equivocal Pathogenic Status
RT   for Cattle.";
RL   Genome Announc. 1:e00348-e00313(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENY68990.1}.
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DR   EMBL; AORH01000034; ENY68990.1; -; Genomic_DNA.
DR   RefSeq; WP_004421576.1; NZ_AORH01000034.1.
DR   AlphaFoldDB; N9TSC5; -.
DR   STRING; 1188235.MBVG_6680; -.
DR   PATRIC; fig|1188235.3.peg.666; -.
DR   eggNOG; COG0446; Bacteria.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000013220; Unassembled WGS sequence.
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; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 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; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000013220}.
FT   DOMAIN          1..308
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          333..434
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   454 AA;  50028 MW;  C2308952ADBA18DE CRC64;
     MKIILVGANH AGTSFIRTLK TVNKDAEITA YDRNTNTSFL GCGIAVWVAG EFDEPGGLFY
     SSPESLKQDY GVNLKTNHEV IAIDKAKKQV TVRNNADGST FTDNYDKLVF AGGTWPIEPK
     IKGIEYNKIV LSKLYQHAQK LIEYANDKDI KDVTIVGAGY IGVELVEAFH LKGKKVTLID
     VNKRVTGNYF SEEFTNVMQA NMRKEGIKLA LGEKVVEFRS KNGKDVSSVV TDKGEYKTDL
     VVMCIGFKPR TDFVDLEKLP NGAILVDEFQ RSVSDENIYA VGDSCALKHA VTGDNRHVAL
     ATNAVKSGLV AALHIAGVNV PFPGVAGTNA INVFDCHYAG TGFTEEMAKA NGFEHAASVH
     FEDMDRPEFM REAEKVACTI VYDKQTLKLL GVQLGSWGKT IHAETIYMFA LAIQKGLTLP
     EIALTDVFFL PHFNKPFNFF LVPMLKALGI NYKK
//
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