ID A0A0D0S9P7_9FIRM Unreviewed; 432 AA.
AC A0A0D0S9P7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=P261_01712 {ECO:0000313|EMBL:KIR02897.1};
OS Lachnospiraceae bacterium TWA4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR02897.1, ECO:0000313|Proteomes:UP000032079};
RN [1] {ECO:0000313|EMBL:KIR02897.1, ECO:0000313|Proteomes:UP000032079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR02897.1,
RC ECO:0000313|Proteomes:UP000032079};
RX PubMed=25495654;
RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT "Investigation of a new acetogen isolated from an enrichment of the tammar
RT wallaby forestomach.";
RL BMC Microbiol. 14:314-314(2014).
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:KIR02897.1}.
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DR EMBL; JPZU01000001; KIR02897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0S9P7; -.
DR STRING; 1392836.P261_01712; -.
DR PATRIC; fig|1392836.3.peg.1947; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000032079; 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 ECO:0000313|EMBL:KIR02897.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000032079}.
FT DOMAIN 4..369
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 432 AA; 48808 MW; 46991EADDCD6101D CRC64;
MKTDVLIVGS GCSGLYCAMN LPRDKQILII TKSDLESNDS FLAQGGMCVL KSKEDYQSYF
EDTLKAGHYE NDKKSVEIMI KNSPDVLADL ISYGADFQKD RAGNLIYTKE GAHTHPRIVY
HEDVTGREIT STLLHKVKEL DNVTFLEYTT LVDLICENNC CYGGVVRTKD GKIQSIEADH
TVLATGGIGG LYKHSTNFKH LTGDSLAIAL KHGIELEHVD YIQIHPTTLY SDKPEDRSFL
ISESVRGEGA KLYDKNGHRF VDELLPRDLL TQKIHEQMEK DGTDYVWEDL RTIPEEELKN
HFPNIIEHCK QMGYDVFKEC IPVVPAQHYF MGGIKVNHES HTSMEHLYAV GETACNGVHG
RNRLASNSLL ESLVFAKRAA GEIANCKVHL YHEPIDIDKE AYIDLENKYR ELVLTEIERQ
SHKYVRSSNI GA
//
