ID A0A0F2DET0_STRMT Unreviewed; 459 AA. AC A0A0F2DET0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 27-NOV-2024, entry version 25. DE RecName: Full=NADH oxidase {ECO:0000256|ARBA:ARBA00039201}; DE EC=1.6.3.4 {ECO:0000256|ARBA:ARBA00039092}; GN Name=nox {ECO:0000313|EMBL:KJQ68734.1}; GN ORFNames=TZ90_01106 {ECO:0000313|EMBL:KJQ68734.1}; OS Streptococcus mitis. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=28037 {ECO:0000313|EMBL:KJQ68734.1, ECO:0000313|Proteomes:UP000033538}; RN [1] {ECO:0000313|EMBL:KJQ68734.1, ECO:0000313|Proteomes:UP000033538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT25 {ECO:0000313|EMBL:KJQ68734.1, RC ECO:0000313|Proteomes:UP000033538}; RA Haase E.M.; RT "Evolution of amylase-binding proteins of oral streptococcal species."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 NADH + O2 + 2 H(+) = 2 NAD(+) + 2 H2O; 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:0000256|ARBA:ARBA00036014}; 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:KJQ68734.1}. 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; JYGP01000002; KJQ68734.1; -; Genomic_DNA. DR RefSeq; WP_045611922.1; NZ_JYGP01000002.1. DR AlphaFoldDB; A0A0F2DET0; -. DR GeneID; 61380852; -. DR PATRIC; fig|28037.212.peg.1072; -. DR Proteomes; UP000033538; Unassembled WGS sequence. 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; IPR050260; FAD-bd_OxRdtase. 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; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Oxidation {ECO:0000256|ARBA:ARBA00023097}; KW Oxidoreductase {ECO:0000313|EMBL:KJQ68734.1}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}. FT DOMAIN 3..319 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 349..444 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" SQ SEQUENCE 459 AA; 50262 MW; 1B839EA64EF22D8B CRC64; MSKIVVVGAN HAGTACINTM LDNFGNENEI VVFDQNSNIS FLGCGMALWI GEQIDGAEGL FYSDKEKLEA KGAKVYMKSP VLSIDYDNKV VTAEVEGKEH KESYEKLIFA TGSTPILPPI EGVEIVKGNR EFKATLENVQ FVKLYQNAEE VINKLADKSQ HLDRIAVVGG GYIGVELAEA FERLGKEVVL VDIVDTVLNG YYDRDFTQMM AKNLEDHNIR LALGQTVKAI EGDGKVERLI TDKETFDVDM VILAVGFRPN TALADGKIEL FRNGAFLVNK KQETSLPGVF AVGDCATVYD NARKDTSYIA LASNAVRTGI VGAYNACGHE LEGIGVQGSN GISIYGLHMV STGLTLEKAK AAGYNATETG FNDLQKPEFM KHDNHEVAIK IVFDKDSREI LGAQMVSHDP AISMGIHMFS LAIQEHVTID KLALTDLFFL PHFNKPYNYI TMAALTAEK //