ID J6H9Z7_9FIRM Unreviewed; 444 AA.
AC J6H9Z7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:EJU21995.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:EJU21995.1};
GN Name=noxE {ECO:0000313|EMBL:EJU21995.1};
GN ORFNames=HMPREF1143_0867 {ECO:0000313|EMBL:EJU21995.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU21995.1, ECO:0000313|Proteomes:UP000005244};
RN [1] {ECO:0000313|EMBL:EJU21995.1, ECO:0000313|Proteomes:UP000005244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU21995.1,
RC ECO:0000313|Proteomes:UP000005244};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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}.
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:EJU21995.1}.
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DR EMBL; ALNK01000025; EJU21995.1; -; Genomic_DNA.
DR RefSeq; WP_009531211.1; NZ_ALNK01000025.1.
DR AlphaFoldDB; J6H9Z7; -.
DR PATRIC; fig|796941.3.peg.1426; -.
DR Proteomes; UP000005244; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PRINTS; PR00411; PNDRDTASEI.
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 Oxidoreductase {ECO:0000313|EMBL:EJU21995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005244}.
FT DOMAIN 3..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 331..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 444 AA; 48433 MW; 50F48D99E5365F39 CRC64;
MSKIVVVGAN HAGTAAINTI TGFNENNEVV VFDQNSNISF LGCGMALWIG EQISKPDGLF
YSNKEKLESQ GAKINMNSSV DSVDFDKKIV HATLENGQKI EESYDKLILA TGSLPIVPNV
KGKDLENVQM VKLFQNAEDV IEKLKNPEIK TVAVVGAGYI GVELAEAFER KGKKVVLIDT
MSTALSNYYD IEFSTMMDKN LESHGIQLAY GEMVKEIIGT TKVEGIITDK NQYKCDMVIL
AVGFRPNTAL GGGKLKTLAN GAYLVDETQQ TNVKDVYAIG DCASVLFNST GENSYIALAT
NAVRSGLIAG HNVCGKHMET NGVQGSNGIA IYDLKMVSTG LSEERAKKLG LEVESTSFED
LQKAAFIETE NPKVKIKIVY DKNTRVVIGA QMASTYDMSM GIHMFSLAIQ EKVTIDRLKL
LDILFLPHFN QPYNYITMAA LSAK
//
