ID A0A0F0C883_9CLOT Unreviewed; 552 AA.
AC A0A0F0C883;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=L-aspartate oxidase {ECO:0000313|EMBL:KJJ69990.1};
DE EC=1.4.3.16 {ECO:0000313|EMBL:KJJ69990.1};
GN Name=nadB_2 {ECO:0000313|EMBL:KJJ69990.1};
GN ORFNames=CLFS41_33370 {ECO:0000313|EMBL:KJJ69990.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ69990.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ69990.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ69990.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
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:KJJ69990.1}.
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DR EMBL; JYHN01000062; KJJ69990.1; -; Genomic_DNA.
DR RefSeq; WP_052665792.1; NZ_JYHN01000062.1.
DR AlphaFoldDB; A0A0F0C883; -.
DR PATRIC; fig|1609975.3.peg.3577; -.
DR Proteomes; UP000033604; 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 GO; GO:0019363; P:pyridine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; 2.
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:KJJ69990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT DOMAIN 6..402
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 457..542
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 552 AA; 60771 MW; 32A12A16F65AEAEA CRC64;
MNITIDILVI GAGGAGCRAA IAAADCGTSV LLASKKPLGE SGATSYPVAE MAGYNAGDVS
IPMDVQMHYN DIIEAGQGMA DEELAAIVAS RAPETIRQLE EWGVKFEHEN EGYYVFRSCF
SHYPRTHVIK GHGEPVVRAM KDQIHARPNI TVMDDVTIMG LYVRDGCCVG ACGLAGREMV
YINSKAVILA SGGCGQAFER NMNPSDVTGG GYSMAYHAGA DLVNMEFMQI GMGFSWPVVN
IFNGYIWETK PRLSDREGKD IFEEVLPQNL TPDQVMHEHR KHFPFSSSDD SKYLEVAVQT
AVKNGRGTQR GGIRADFSHI TDEYVNSLKD DCGIHHMWPI ARDYLRSRGV DLLLDQVEVA
CYAHAINGGV RINTKGMSSI QGLYAAGECA GGPHGADRLG GNMMVTCQVF GEIAGTSAAE
YALRTQHAEH VEHLRDPHME EMKALLYRKL DCMGMLNRLR KAAQDNLLVA RTEDGLTQVL
NVAGELEGEM VHADTCQEIY PENIDLYHML TTVRIMARCA LERRESRGSH HRADHPFKDE
RFNKPVTIRK NG
//
