ID A0A0H3XJC2_9MOLU Unreviewed; 452 AA.
AC A0A0H3XJC2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AKM53921.1};
GN Name=nox {ECO:0000313|EMBL:AKM53921.1};
GN ORFNames=SERIO_v1c03390 {ECO:0000313|EMBL:AKM53921.1};
OS Spiroplasma eriocheiris.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=315358 {ECO:0000313|EMBL:AKM53921.1, ECO:0000313|Proteomes:UP000035661};
RN [1] {ECO:0000313|EMBL:AKM53921.1, ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RX PubMed=26254485; DOI=10.1093/gbe/evv160;
RA Lo W.S., Gasparich G.E., Kuo C.H.;
RT "Found and Lost: The Fates of Horizontally Acquired Genes in Arthropod-
RT Symbiotic Spiroplasma.";
RL Genome Biol. Evol. 7:2458-2472(2015).
RN [2] {ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RA Lo W.-S., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma eriocheiris TDA-040725-5 (DSM
RT 21848).";
RL Submitted (JUN-2015) 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}.
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DR EMBL; CP011856; AKM53921.1; -; Genomic_DNA.
DR RefSeq; WP_047791179.1; NZ_CP011856.1.
DR AlphaFoldDB; A0A0H3XJC2; -.
DR STRING; 315358.SERIO_v1c03390; -.
DR KEGG; seri:SERIO_v1c03390; -.
DR PATRIC; fig|743698.3.peg.340; -.
DR Proteomes; UP000035661; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035661}.
FT DOMAIN 1..307
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..430
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 452 AA; 50163 MW; 5794B3F3EBF8D9B9 CRC64;
MKVIVVGTNH AGTTAVRTLR RLDPSAEIVT YDKNNNVSFL GCGIALWVKG EVQDPQGLFY
ASPEILESEG IKVNMEHEVL NIDNKKKTIH VKDLKTGKEF DDNYDRLILA IGSWPIIPPI
EGITMEGVHI VKWYQHGALV KKANEDPNIK NVVVCGAGYI GVELVDAFHA KGKNVTLVDI
SDRIMPRYYD KPFTDRVENA MKAAGVHLAT GEKVMKFEGE NNKVTKVVTD KGSHAADMVI
WAVGFKPATE MLAGVVDLDN NKAIMVNEFM QTSDENIFAV GDCIEVYDNA KQRPCYIALA
TNAVRTGIIA AVNALKPAGL ASPGFQGSNA INVFDWCLAS TGVTETVAKE LGMDYEQITF
EDNDRPEFMH SYKKVLIKIL WDKKTRKIIG AQVGSENNHT EVMYMFSLAI MKGVTIDELP
LIDIFFLPHF NKPYNFITLP ALEVLGLNYF KK
//
