ID A0A0S2KDQ1_9GAMM Unreviewed; 542 AA.
AC A0A0S2KDQ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=PS2015_1601 {ECO:0000313|EMBL:ALO46254.1};
OS Pseudohongiella spirulinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO46254.1, ECO:0000313|Proteomes:UP000065641};
RN [1] {ECO:0000313|EMBL:ALO46254.1, ECO:0000313|Proteomes:UP000065641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO46254.1,
RC ECO:0000313|Proteomes:UP000065641};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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; CP013189; ALO46254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2KDQ1; -.
DR STRING; 1249552.PS2015_1601; -.
DR KEGG; pspi:PS2015_1601; -.
DR PATRIC; fig|1249552.3.peg.1607; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000065641; 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 PRINTS; PR00411; PNDRDTASEI.
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:UP000065641}.
FT DOMAIN 5..399
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 449..529
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 542 AA; 60147 MW; 1B7AB752E87A7718 CRC64;
MYDYDILIIG SGAAGLSLAL KTASFARVAV LSKGSLNQGA TFWAQGGIAA VLDENDSVDA
HIADTLDAGA GLCNEDMVRH VVEHSQQAIQ WLVEQGVPFT VMSREEAGTG AASEPLNADN
LKPLHLTQEG GHSHRRIIHA TDATGRAIFE TLLRQAQQTS GITLYENRLA VDLITRQKLG
LEGNDCVGAY VYNNESRSVE VFRARFVVLA SGGASKAYLY TTNPESATGD GIAMAWRAGC
RVANMEFNQF HPTCLYHPHA RSFLITEALR GEGATLELPA GSRFMPAFDE RAELAPRDIV
ARAIDHEMKR LGCDCVYLNI SHKPAAFIRE HFPTIYARCL EFGIDITRDR IPVVPAAHYT
CGGVMVDKLG RTDINHLYAI GETSCTGLHG ANRMASNSLL ECFVLAFGAA DDIRTHIDRL
PAAPEKIPDW DESRVTQSQE EVIVAHNWDE LRRVMWDFVG IVRSDQRLLK ARRRIQMLEH
EISYHYRHYL ISRDLLELRN LVQVSRLIVE SALLRKESRG LHYTIDYPDL ARSASDTVLT
PQ
//
