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Database: UniProt
Entry: A0A0J1FBA2_9FIRM
LinkDB: A0A0J1FBA2_9FIRM
Original site: A0A0J1FBA2_9FIRM 
ID   A0A0J1FBA2_9FIRM        Unreviewed;       666 AA.
AC   A0A0J1FBA2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=L-aspartate oxidase {ECO:0000313|EMBL:KLU60675.1};
DE            EC=1.4.3.16 {ECO:0000313|EMBL:KLU60675.1};
GN   Name=nadB_3 {ECO:0000313|EMBL:KLU60675.1};
GN   ORFNames=CEB3_c30580 {ECO:0000313|EMBL:KLU60675.1};
OS   Peptococcaceae bacterium CEB3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU60675.1, ECO:0000313|Proteomes:UP000035957};
RN   [1] {ECO:0000313|EMBL:KLU60675.1, ECO:0000313|Proteomes:UP000035957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEB3 {ECO:0000313|EMBL:KLU60675.1,
RC   ECO:0000313|Proteomes:UP000035957};
RA   Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA   Muehling M.;
RT   "Genome sequence of the moderately acidophilic sulfate reducing
RT   Peptococcaceae bacterium strain CEB3.";
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   -!- 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:KLU60675.1}.
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DR   EMBL; LDXJ01000059; KLU60675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1FBA2; -.
DR   STRING; 999898.CEB3_c30580; -.
DR   PATRIC; fig|999898.3.peg.3439; -.
DR   Proteomes; UP000035957; Unassembled WGS sequence.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KLU60675.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035957}.
FT   DOMAIN          51..488
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          547..648
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   666 AA;  72863 MW;  5673CE4027E5FDA9 CRC64;
     MSVFDHRLNR PFSAGQVQKK VETYEYHDYP HYLRIRCSGM EVLAVAQFSC DVLIVGGGGG
     ALRAAIAAKE RCPESDVLLV SKGVLGQSGV TATACSDRMA FHATLPHTPP GKADNWRFHA
     EDIYRIGGQV SDWDLAEILA KESAAAYDYL DELGVPFVKE GLVPKQFATD GSEYPRACYT
     GPRTAVEIER HLLKRFRALG IRVLEHVMVA ELIREGSKII GALAIDERVR EDSAGEEDGF
     IVPIAAKTVI LATGGAGLIY KNNVFPAGMS GDGYVLAYEA GAELVNLEFI QIGVASLKTK
     LNLSGSLLRA VPRLVDETGT EFLASYFPPG TNPAVLHDYI FRKGASWPVS FEHDTRLIDL
     AISRRMREGH RVFLDYSHNP EQFDFGHLPE RDRAGYAEEM VADFGAEARQ ASPLARLQEI
     NPASVSWLKE HGINLMAGDK VEVAACGQHF QGGVKIGPNG ESTLPGLYAV GEAAGGQHGA
     NRPGGNALLD SQVFGKIAGE AAARESRGII RASIPAEVVT SFRHEMERLS RNQGERPDSR
     LSVRDARKGL QEIVDASVGV VRTEAGLRRG LAELEKLRNK GMTLAGLPYT LGLETRNMFT
     VAEMVMRAAL ERNESRGPHL RFSDEDSDVP LPRLDPEWQR YLVLYRKEGE MVVEGRAPIK
     SGCDRD
//
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