ID A0A0K1JVU8_9BURK Unreviewed; 537 AA.
AC A0A0K1JVU8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ACZ75_05980 {ECO:0000313|EMBL:AKU21101.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU21101.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU21101.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU21101.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-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}.
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DR EMBL; CP012201; AKU21101.1; -; Genomic_DNA.
DR RefSeq; WP_050407878.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1JVU8; -.
DR STRING; 1678028.ACZ75_05980; -.
DR KEGG; mnr:ACZ75_05980; -.
DR PATRIC; fig|1678028.3.peg.1219; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000056897; 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 PIRSF; PIRSF000171; SDHA_APRA_LASPO; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056897}.
FT DOMAIN 4..393
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 440..520
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 452..479
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 537 AA; 58971 MW; C26365D5FE4F6016 CRC64;
MKFDVAIVGS GLAGLSVALH LAETRKVAII SKRALLDGAS NWAQGGIAAV LDSGDSHEQH
IADTLVAGGG LCDEGATRFI VENGRSAIEW LIAQGVPFTR DDSAELGFHL TREGGHSQRR
IIHAADATGH AVQVTLEEKV RAHPNISLFE HHCAIDLITT DKLGPRPGHS QPKCHGLYVQ
DTKTGQVLTF AAEHTVMATG GAGKVYLYTT NPDTASGDGI AMAWRAGCRV SNMEFIQFHP
TCLYHPYAKS FLITEAIRGE GGLLKLPPEA GAAAGQRFML AHDERAELAP RDVVARAIDF
EIKKRGLDYV HLDISHKPAE FLIEHFPTIY ARCLELGIDI TKEAIPIVPA AHYTCGGVVT
DLLGRTDLPG LYAVGETACT GLHGANRLAS NSLLECVVVG RACADDILSK EKVDAPYLPD
WDESRVSDAD EEVVIAHNWD ELRRFMWNYV GIVRTTKRLE RAQHRIALLK EEIDEYYRNF
RITHDLLELR NLVDVASMIV NSALQRRESR GLHFSRDYPD TLPKALPSVL TPSRRRN
//
