ID A0A1I4C367_9BACL Unreviewed; 534 AA.
AC A0A1I4C367;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN03159341_101423 {ECO:0000313|EMBL:SFK75522.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFK75522.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFK75522.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFK75522.1,
RC ECO:0000313|Proteomes:UP000198699};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOTE01000001; SFK75522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4C367; -.
DR STRING; 1566278.SAMN03159341_101423; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000198699; Unassembled WGS sequence.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
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 Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal 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 15..371
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 435..515
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 534 AA; 57724 MW; 74A8C93BE5533173 CRC64;
MSNHSKNNER SLEADVLILG GGPAGTWAAV AAAEAGASVI LADKGYCGTS GATAPSGNNI
WVAHPDPELH EKAMQDRHRL GGFLSDRAYL NPVLAQTVVN RSRLEAWKFP FHYNQAGETI
YSLQGPEYMK MMRSRVKRAG VKIMDHCPAT ELLADDEGVC GAAGIMLDNG ERWSVKAHAV
IIATGGCAFL SKALGCNVLT GDGLLMAVEA GAELSGMEFS NTYGICAANS SVTKNAFFSY
GSYTYEDGSR VEGTDAADDA IVPAKIFTIQ SAIAKKLKDH TIYCKFDKAG EAMRPQMRKG
QPNLFLAFDR LGIDPFKDRF PVTLRLEGTV RGTGGINILD QTCATRVPGL YAAGDAATRE
HMAGGFSGGG SHNAAWAMSS GVFSGQAAAR FASTLGQHGR KRNFKGLAGG SETGSGQRTY
QAERNTDYIR AIQEEVMPYD KNFFRSETKL RSSLSNLHEV WSALRATSAP TGVQQVKFRE
ATAMAAVSRW MYTSALNRTE SRGMHQYEDY PHLDQAQQRR LLSGGLDQVW VKPL
//
