ID A0A1W2DNK0_9RHOB Unreviewed; 521 AA.
AC A0A1W2DNK0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN ORFNames=SAMN06295998_11624 {ECO:0000313|EMBL:SMC98963.1};
OS Primorskyibacter flagellatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Primorskyibacter.
OX NCBI_TaxID=1387277 {ECO:0000313|EMBL:SMC98963.1, ECO:0000313|Proteomes:UP000192330};
RN [1] {ECO:0000313|EMBL:SMC98963.1, ECO:0000313|Proteomes:UP000192330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12644 {ECO:0000313|EMBL:SMC98963.1,
RC ECO:0000313|Proteomes:UP000192330};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562}.
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DR EMBL; FWYD01000016; SMC98963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2DNK0; -.
DR STRING; 1387277.SAMN06295998_11624; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000192330; Unassembled WGS sequence.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
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 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000192330}.
FT DOMAIN 9..380
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 462..494
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 521 AA; 52698 MW; 542426AA329D4EBF CRC64;
MAAIDTPRAI IVGAGLAAQY AALRLAPHPV LMISPEPLGS GASSAWAQGG VAAAMDPSDS
AEAHARDTVR AGAGTVDVQV AEAVTAEARA HILDLTGLGT PFDRTADGGY VLSREAAHSF
ARVVRVRGDQ AGSEIMQALT AQVRAAPHVQ VLEGVMATGL VIEGGRVYGA RVARCADGLT
QSVALRGAAV LLAGGGSGSL FSQTTNPPRI CGQVLGMAAR AGAVISDAEF VQFHPTAIAN
GLDPAPLATE ALRGEGATLI NSRGERFMLA AHPDAELAPR DIVARAVFAQ TQAGLAPALD
TRAALGARIL TEFPAVAAAC RASGLDPVAQ PIPVAAAAHY HMGGIATDAG GASTLPGLWA
CGEVASTGLH GANRLASNGL LEALVYGRRC ADAIGKGLGA GDVAPVELPD LAPAQAPDPA
LVARLRQAMT DGAGVIRTAA GLRRTLDTIA TIAAAQPDCD ALLNMTATAT LIAAAALARK
ESRGAHFRSD HPDVQGATGE RSFFTLAQAQ EIRAQARKEP A
//
