ID A0A0F2DVV6_9STRE Unreviewed; 459 AA. AC A0A0F2DVV6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 14-DEC-2022, entry version 21. DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:KJQ74080.1}; DE EC=1.6.-.- {ECO:0000313|EMBL:KJQ74080.1}; GN Name=nox {ECO:0000313|EMBL:KJQ74080.1}; GN ORFNames=TZ94_01601 {ECO:0000313|EMBL:KJQ74080.1}; OS Streptococcus infantis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=68892 {ECO:0000313|EMBL:KJQ74080.1, ECO:0000313|Proteomes:UP000033489}; RN [1] {ECO:0000313|EMBL:KJQ74080.1, ECO:0000313|Proteomes:UP000033489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UC921A {ECO:0000313|EMBL:KJQ74080.1, RC ECO:0000313|Proteomes:UP000033489}; 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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; 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:KJQ74080.1}. 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; JYGT01000010; KJQ74080.1; -; Genomic_DNA. DR RefSeq; WP_045615831.1; NZ_JYGT01000010.1. DR AlphaFoldDB; A0A0F2DVV6; -. DR EnsemblBacteria; KJQ74080; KJQ74080; TZ94_01601. DR PATRIC; fig|28037.216.peg.1569; -. DR Proteomes; UP000033489; 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 GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 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 Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. PE 4: Predicted; KW Oxidoreductase {ECO:0000313|EMBL:KJQ74080.1}. FT DOMAIN 3..319 FT /note="Pyr_redox_2" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 349..444 FT /note="Pyr_redox_dim" FT /evidence="ECO:0000259|Pfam:PF02852" SQ SEQUENCE 459 AA; 50286 MW; A7CEB1A391972CE5 CRC64; MSKIVVVGAN HAGTACINTM LDNFGNENEI VVFDQNSNIS FLGCGMALWI GEQIDGAEGL FYSDKEKLEA KGAKVYMNSP VLSIDYDNKV VTAEVEGQEH KESYEKLIFA TGSTPILPPI EGVEIVKGNR EFKATLENVQ FVKLYQNAEE VINKLADKSK HLERIAVVGG GYIGVELAEA FERLGKEVVL VDIVDTVLNG YYDKDFTQMM AKNLEDHNIR LALGQTVKAI EGEGKVERLI TDKETFDVDM VVLAVGFRPN TALADGKIEL FRNGAFLVDK KQETSIPGVY AVGDCATVYD NARKDTSYIA LASNAVRTGI VGAYNACGHE LEGIGVQGSN GISIYGLHMV STGLTLEKAK AAGYNATETG FNDLQKPEFM KHDNYEVAIK IVFDKDSREI LGAQMVSRDS AISMGIHMFS LAIQEHVTID KLALTDLFFL PHFNKPYNYI TMAALTAEK //