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
//