ID A0A0B4XP72_9GAMM Unreviewed; 525 AA.
AC A0A0B4XP72;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901, ECO:0000256|RuleBase:RU362049};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN ORFNames=S7S_12445 {ECO:0000313|EMBL:AJD48901.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD48901.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD48901.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD48901.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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; CP004387; AJD48901.1; -; Genomic_DNA.
DR RefSeq; WP_008738766.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XP72; -.
DR STRING; 391936.S7S_12445; -.
DR KEGG; apac:S7S_12445; -.
DR HOGENOM; CLU_014312_3_0_6; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000006764; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006764}.
FT DOMAIN 7..381
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 430..512
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 442..469
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 525 AA; 58197 MW; B286C5C4F664BE36 CRC64;
MATYRHDVLI IGSGAAGLTV ALRMSPDARI ALLSKGELTS ASTYYAQGGV AAVMDQQDSL
ESHIKDTHVA GAGLCHEDAV RKTVENGPDA IRWLIDQGVG FTRFEEDGRQ GFHLTREGGH
SHRRVIHVAD ATGLAISGAL IDQVGRRQNV ELFEHRTAVD LIVQDGRCAG AYIHNPITGR
TDVFLARAVV LATGGASKVY LYTSNPDVAT GDGIAMAWRA GCRVSNMEFM QFHPTCLYHP
KAKSFLVTEA IRGEGGHLLL PDGSRFMHQF HERGELAPRD VVARAIDFEM KRLGADCLYL
DISHRPADFI INHFPTVYAK CLQLGIDITR DPIPVVPAAH YTCGGVITDM HGRTDLPGLY
AIGETAFTGL HGANRMASNS LLECFVFGQA ASEDISAQLK TLPEPRNAPE WDDSLVTDSD
EDVIISHNWD ELRRFMWDYV GIVRTVKRLE RAMHRIDLLK REIAEYYSNY RISSDLLELR
NLVVIGELII RSALQRRESR GLHYILDFPE MEAEAKDTIL VPDQD
//
