ID E4L0K3_9FIRM Unreviewed; 420 AA.
AC E4L0K3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=HMPREF9286_0846 {ECO:0000313|EMBL:EFR32395.1};
OS Peptoniphilus harei ACS-146-V-Sch2b.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR32395.1, ECO:0000313|Proteomes:UP000003705};
RN [1] {ECO:0000313|EMBL:EFR32395.1, ECO:0000313|Proteomes:UP000003705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR32395.1,
RC ECO:0000313|Proteomes:UP000003705};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-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}.
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:EFR32395.1}.
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DR EMBL; AENP01000027; EFR32395.1; -; Genomic_DNA.
DR RefSeq; WP_005957775.1; NZ_AENP01000027.1.
DR AlphaFoldDB; E4L0K3; -.
DR eggNOG; COG0029; Bacteria.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000003705; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003705}.
FT DOMAIN 5..363
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 420 AA; 47025 MW; 6597C3FBE45D45EC CRC64;
MKKFDVLIVG SGLAGVSTAL ELSKDYKIGL VTKKNLEDSN SYLAQGGINV LRDDDDRQVF
IEDTMKAGHY KNDLKSVETM VDKSQEAIEF LMDLGVEFTK KDGQLDYARE GGHSASRGLH
IDDEIGKGIL DVLYKRLIER SNIEIFEDTP ILDLIVKDGK CYGARSRDEV FISTNVVLAT
GGLGGLFDKS TNFPHISGDG LAMAIKNGVK IKDISYIQFH PTSLYEEGVE RQLLISESAR
GEGAVLLNHE DQRFTDEMKP RDIVAGAIKN EMEREGVDFE YLSMKPLGEE RIPKRFPMIF
DELKARGIDP RYENIPIVPC QHYTMGGIEC DIEGRTNLEG LFVVGEAGNV GIHGSNRLAC
NSLLECLVFG RILADYLNEN KLEEKEIDFT IDTKDLDGED KKKIIFERIR EDERAKANLN
//
