ID Q8R649_FUSNN Unreviewed; 435 AA.
AC Q8R649;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AAL95284.1};
DE EC=1.6.-.- {ECO:0000313|EMBL:AAL95284.1};
GN OrderedLocusNames=FN1088 {ECO:0000313|EMBL:AAL95284.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL95284.1, ECO:0000313|Proteomes:UP000002521};
RN [1] {ECO:0000313|EMBL:AAL95284.1, ECO:0000313|Proteomes:UP000002521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL95284.1; -; Genomic_DNA.
DR RefSeq; NP_603985.2; NC_003454.1.
DR AlphaFoldDB; Q8R649; -.
DR STRING; 190304.FN1088; -.
DR PaxDb; 190304-FN1088; -.
DR EnsemblBacteria; AAL95284; AAL95284; FN1088.
DR KEGG; fnu:FN1088; -.
DR PATRIC; fig|190304.8.peg.1653; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_0; -.
DR InParanoid; Q8R649; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:AAL95284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002521}.
FT DOMAIN 1..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..423
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 435 AA; 48310 MW; 89AE195718CC6C11 CRC64;
MSAASKAKRI DKSLDITVYE MTDAISWGAC GLPYYVGDFY PNASLMVAKT YEEFQKEGIN
VKIKHKVENI DFKNKRIFVR NLNENKVFED NYDKLVIATG ASSTSPKDIK NLDAEGVYHL
KTFNEGLEVK KEMMKKENEN IIIIGAGYIG IEIAEAALKL GKNVRIFQHS ARILNKTFDK
EITDLLENHI REHEKISLHL NESPVEVRTF EDKVIGLKTD KKEYVANLII VATGVKPNTE
FLKDTGIELF KNGAIIINRF GETNIPNVYA AGDCATVYHS VLEKNVYIAL ATTANKLGRL
IGENLTGTNK VFIGTLGSAG IKVLEFEAAR TGITEQEAKD NNINYKTIFV DGEDHSAYYP
GGEDVYIKLI YNADTKILLG AQLAGKRGAA LRTDSLAVAI QNKMTVQELA NMDFLYAPPF
ATTWDIMNVA GNVAK
//
