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
//