ID A0A1Q8Q809_9BACI Unreviewed; 528 AA.
AC A0A1Q8Q809;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BTO30_05820 {ECO:0000313|EMBL:OLN23476.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN23476.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN23476.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN23476.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
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}.
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:OLN23476.1}.
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DR EMBL; MSDU01000008; OLN23476.1; -; Genomic_DNA.
DR RefSeq; WP_075397767.1; NZ_MSDU01000008.1.
DR AlphaFoldDB; A0A1Q8Q809; -.
DR STRING; 1714264.BTO30_05820; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000185568; Unassembled WGS sequence.
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 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 7..371
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 413..492
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 528 AA; 58030 MW; F64C98BD19C1353D CRC64;
MKFSSQVVII GSGIAALQAA KHLGVQVNVI VITKSVIRDS NSYYAQGGIA AVLSTDDTYD
SHMQDTFEAG EYHHSLSNVQ QLITEGANAV KELLQEGFPA DYRSDGTLSL CLEGAHSRHR
IVHSGGDATG KMMIEHFIQS LPDNVRIIER EMAFELIVSN GTCFGVKTKN ADGVIHTYEA
QHTILATGGA GALYPFTSNR KTLTGDGIAL AYRAGVEVTD MEFVQFHPTL LFVNGETKGL
VSEAVRGAGA VLVDENGRRL MRGVHPMEDL APRHITAFEI YKALKKGRNV FLDVSMINDF
QERFPTISAL CLENGIDLKE GLIPVAPGSH FLMGGVKADS YGRTSIARLY AAGETACTGV
HGANRLASNS LLEGIAFGKR MAIHILTYKK KSMNFQPAEQ ARPVQLPPLF EMDELKKRMM
EDAGIIRTKQ GLARMTDCLR IMEGANGDIS GLSIEDMEKL FMHTTAYLIA RAALERTETR
GAHIRADFPE SAPLWRKKWV TFEKGMLSVR GEENEFDQAR PNAYSFFY
//
