ID C0FT15_9FIRM Unreviewed; 388 AA.
AC C0FT15;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=ROSEINA2194_01882 {ECO:0000313|EMBL:EEG94244.1};
OS Roseburia inulinivorans DSM 16841.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=622312 {ECO:0000313|EMBL:EEG94244.1, ECO:0000313|Proteomes:UP000003561};
RN [1] {ECO:0000313|EMBL:EEG94244.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG94244.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG94244.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG94244.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Roseburia inulinivorans (DSM 16841).";
RL Submitted (MAR-2009) 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:EEG94244.1}.
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DR EMBL; ACFY01000084; EEG94244.1; -; Genomic_DNA.
DR AlphaFoldDB; C0FT15; -.
DR eggNOG; COG0029; Bacteria.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000003561; 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 Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}.
FT DOMAIN 4..369
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 388 AA; 43855 MW; ED2AD6A9AAB60EFD CRC64;
MKTDILIVGS GCSGLYAVLN LPEELDIMLI TKSDFESSDS FLAQGGMCTL KDPSDYDSFF
EDTLKAGHYE NDQKSVEIMI KSSPDVVKDL VKYGVSFTRD ENGDFVYTRE GAHAHHRILF
HEDITGKEIT SHLLNAVKKL KNVRMYEYTT LLDILCDGSK CCGGIIRWPD GREEQVEADY
VILATGGIGG TYKHSTNFKH LTGDGVEIAR RHNIELKNLD YVQIHPTTLY SDNKEERSFL
ISESVRGEGA RLYDKNMNRF VDELLPRDLL TQEIYKQMEK DGTDFVWEDL RTIPRDELIS
HFPNIIEHCS QAGYDVFHEC IPIVPAQHYF MGGIKVNHNS KTSMDHLYAV GETACNGVHG
KNRLASNSLL ESLVFAKRAA KEIAGERR
//
