ID A0A3R6VGF1_9FIRM Unreviewed; 429 AA.
AC A0A3R6VGF1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE AltName: Full=Quinolinate synthase B {ECO:0000256|ARBA:ARBA00030386};
GN ORFNames=DXB15_05020 {ECO:0000313|EMBL:RHV70845.1};
OS Roseburia sp. OM02-15.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=2292368 {ECO:0000313|EMBL:RHV70845.1, ECO:0000313|Proteomes:UP000285983};
RN [1] {ECO:0000313|EMBL:RHV70845.1, ECO:0000313|Proteomes:UP000285983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM02-15 {ECO:0000313|EMBL:RHV70845.1,
RC ECO:0000313|Proteomes:UP000285983};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562}.
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:RHV70845.1}.
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DR EMBL; QULX01000004; RHV70845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R6VGF1; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000285983; 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:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; IPR005288; NadB.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:RHV70845.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}.
FT DOMAIN 6..370
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 429 AA; 48276 MW; E0429C0D3D73C897 CRC64;
MKEYYDVIIV GTGAAGLYCA LNLPERKKVL LLTKQKADQS DSFLAQGGIC MLRGEGDYND
YFQDTMRAGH FESDEKAVEL MIRSSNSIIR DLVRRHVDFA RDAQGNLAFT REGAHSQPRI
LFHEDETGKQ ITQTLLDEVN TKDNIEICEY MTMVDLIVKD NVCGGIIIMD EKNEVYPVRA
KHVVLACGGL GGLYQNSTNF PHITGDALGI AMKHQIVLEH LDYIQIHPTT LYSKKPGRRF
LVSESVRGEG ALLLDKNGQR FTDELQPRDT VSKAIFAQME KEGSHCVWED MRPLGKDTIL
KHFPNIYQHC LDEGYDPCKE PIPVVPAQHY FMGGIKVDLG SRTSMKGLYA CGETSCNGVH
GKNRLASNSL LESLVFARRA ADDIMFGEEP EFDASGRLDC SRYEDRDAIL GEYHKAVRSE
IERMKKSHE
//
