ID D4MJL4_9FIRM Unreviewed; 493 AA.
AC D4MJL4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=ES1_08720 {ECO:0000313|EMBL:CBL33947.1};
OS [Eubacterium] siraeum V10Sc8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL33947.1, ECO:0000313|Proteomes:UP000007050};
RN [1] {ECO:0000313|EMBL:CBL33947.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL33947.1,
RC ECO:0000313|Proteomes:UP000007050};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum V10Sc8a.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL33947.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL33947.1,
RC ECO:0000313|Proteomes:UP000007050};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929059; CBL33947.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MJL4; -.
DR KEGG; esr:ES1_08720; -.
DR PATRIC; fig|717961.3.peg.975; -.
DR HOGENOM; CLU_014312_3_0_9; -.
DR BioCyc; ESIR717961:G136L-713-MONOMER; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000007050; Chromosome.
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:CBL33947.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}.
FT DOMAIN 7..378
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 493 AA; 55004 MW; 43A4A3BB034FF204 CRC64;
MKFKEYDVII VGTGVSGLYA ALNLDSSMQI LMLSKRELTL CNSALAQGGV AAVMDTSNDN
YELHIKDTLI AGGYKNNIDN VRILVEQGPK DVKNLLNYGV DFDRKQDGSI DLTLEGGHCR
HRIAHHKDST GFEIVTSLIE GVKKLSNVTI LENTHLLGLT KRGDDFLFDV LHEGKHSYYT
TKNTILATGG IGRVYDYTTN SAIATGDGIQ FAYNMGADIQ HLSYVQFHPT AFADHENREC
FLVSEAVRGE GAYLLNCNKE RFMHKYEPER KELAPRDVVS KDMMKEQKET GSDKFYLDIS
YKDPEFIKNR FPMIYNKVLE KGYDMTKEPI PIYPCQHYLM GGIGVNGHGA TNVKGLYAAG
ECAHTGVHGI NRLASNSLLE ALVFSRLIAE DINKNNTHRE LGTLEADYPS PDGKPLPKGI
RTEIRHIMQR SYFVVPDYVE AAKDIKRVTE LKNLLDNGGF EVTPDYIEAK SLTTVAYIIL
SEVVAEGKEK GII
//
