ID A0A1V4ITC0_9CLOT Unreviewed; 454 AA.
AC A0A1V4ITC0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=nadB {ECO:0000313|EMBL:OPJ63045.1};
GN ORFNames=CLORY_14110 {ECO:0000313|EMBL:OPJ63045.1};
OS Clostridium oryzae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ63045.1, ECO:0000313|Proteomes:UP000190080};
RN [1] {ECO:0000313|EMBL:OPJ63045.1, ECO:0000313|Proteomes:UP000190080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ63045.1,
RC ECO:0000313|Proteomes:UP000190080};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium oryzae DSM 28571.";
RL Submitted (MAR-2017) 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:OPJ63045.1}.
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DR EMBL; MZGV01000011; OPJ63045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4ITC0; -.
DR STRING; 1450648.CLORY_14110; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000190080; 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 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:OPJ63045.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000190080}.
FT DOMAIN 9..375
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 454 AA; 50535 MW; 4C1DCDB09BBB6017 CRC64;
MIIMDINSDV LIVGTGAAAL YCSLNLRKDL DVVMLCKSSI TESNSYLAQG GIATALNDND
IKPFMEDTLT AGNNKNDLSA VKILCSESRE VISSLIDLDV PFNRDSSTGN ILYTREGAHR
INRIVYCEDS TGKSVVETLL QHVKKRKNIT IYDYTTVIDL LCKNDNCTGI VAFNQSGKQI
NFYAKTVILA CGGIGGLFKN STNQRTITGD GLFMALKHNI KLKDIQYIQF HPTALYEENP
QSRRFLISES VRGEGGKLYN VKGKRFVNEL LPRDVVAKAI NEQISKYKCP YVFLDVSFLN
KDFLLKRFPL INSECKKRGI DITKDMIPVS PAQHYFMGGI DVDKCSKTSM NNLYAVGEAS
CTGVHGSNRL ASNSLLEGLV FSKRAAGDIN NKIDNINIDT SNSAVISETL PQLSVKQQNL
VIKELEKRCD FLNDEFFISR PSSPRCSERR YSMV
//
