ID A0A0M0GP81_9BACI Unreviewed; 517 AA.
AC A0A0M0GP81;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=AF331_01440 {ECO:0000313|EMBL:KON91231.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON91231.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-2015) 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:KON91231.1}.
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DR EMBL; LGUE01000001; KON91231.1; -; Genomic_DNA.
DR RefSeq; WP_053426448.1; NZ_LGUE01000001.1.
DR AlphaFoldDB; A0A0M0GP81; -.
DR STRING; 189381.GCA_900166615_04026; -.
DR GeneID; 42290593; -.
DR PATRIC; fig|189381.12.peg.366; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000037405; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037405}.
FT DOMAIN 5..365
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 406..512
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 517 AA; 55983 MW; 3210EF85808167FA CRC64;
MRKADVLIIG SGVAALQLAK NIQDRMNVMI ITKSRVKSSN SYMAQGGIAA ALSPDDSPGL
HMKDTLIAGE DLQEEGRVMS FVEDGKRAVE ALLSDGMPFD PELGMEGAHS TKRIVHSGGD
QTGRFLIDFL ISSLSENVKI IEGEMAYHLL KDRNGRIGGV RTKDEAGVIH TYTGDHIVLA
SGGVGGIYAS TSNHPSVTGT GIAMACLAGA VVGDMEFIQF HPTLLLSTGR TKGLISEAVR
GEGGVLVRED GRALMESIHP LKDLAPRHVV AEAIYRERLG GGNVYLDITG IQNFSTRFPS
ITVRCEKEGI PIEGGRIPVA PGCHFIMGGV VVDDVGRTNL DGLYAIGEAA CTGVHGANRL
ASNSLLEGIV YGQRLADHLK EALPPKTAPL AHAPITGTPG QLPDRTMLKK RMMEEAGIIR
SEEGLQRLMQ WLDGFGLTYE SKMDDLDVED MEDYLIWVVS RLIGTASLLR EESRGGHIRR
DHPEKRPEWD KKSIHMKIQT GRLKVSVYES VETKIHA
//
