ID A0A1L6FEA4_9RHOO Unreviewed; 533 AA.
AC A0A1L6FEA4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN ORFNames=Tchl_2394 {ECO:0000313|EMBL:APR05232.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR05232.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:APR05232.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR05232.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CC {ECO:0000256|RuleBase:RU362049}.
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 ECO:0000256|RuleBase:RU362049};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950, ECO:0000256|RuleBase:RU362049}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562,
CC ECO:0000256|RuleBase:RU362049}.
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DR EMBL; CP018839; APR05232.1; -; Genomic_DNA.
DR RefSeq; WP_075149708.1; NZ_FNVJ01000001.1.
DR AlphaFoldDB; A0A1L6FEA4; -.
DR STRING; 96773.Tchl_2394; -.
DR KEGG; tcl:Tchl_2394; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000185739; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-UniRule.
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; 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 NCBIfam; TIGR00551; nadB; 1.
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 PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362049};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362049};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362049};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU362049}.
FT DOMAIN 6..385
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 432..512
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 444..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 533 AA; 58654 MW; 0F8E6CD083CC0A81 CRC64;
MLKQYDVLIL GSGTAGQSIA LRLADTLRVA LVTKRELSDS ASNWAQGGIA AVLDTTDSIE
AHIQDTFTAG AGLCDPGATR FVVENGKRAI DWLIERGVPF TREPDSEFGY HLTREGGHSH
RRVIHAADAT GAAVQLTLSA QVRAHPNIDI YEHHIAVDLV LGDKVGQPGE GCLGAYVLDI
AADEVVTFSA RNTVLATGGT GKVYLYTTNP DVATGDGVAM AWRAGCRVGN MEFIQFHPTC
LYHPQAKSFL ISEAVRGEGG LLKLPDGTRF MPEHDPRAEL APRDVVARAI DFEMKKRGLD
CVYLDISHKP EAWLREHFPN IHARCLELGI DISREPIPVV PCVHFSCGGI VTDLSARTDV
PGLYAVGESA FTGLHGANRL ASNSLLECLV FGEAAARDIL AKPHALPPAL PDWDESRVTD
ADEEVVIAHN WAELRRAMWD YVGIVRTTKR LKRAQHRIRL LEREIHEFYT NFRVSNDLIE
LRNLVTTADL IVRCALRRKE SRGLHTSRDF PTMLARARNT VLRPRPTRKK AGS
//
