ID A0A285SF32_9RHOB Unreviewed; 520 AA.
AC A0A285SF32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN ORFNames=SAMN05877831_10533 {ECO:0000313|EMBL:SOC06497.1};
OS Rhodobacter maris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=446682 {ECO:0000313|EMBL:SOC06497.1, ECO:0000313|Proteomes:UP000219111};
RN [1] {ECO:0000313|Proteomes:UP000219111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA276 {ECO:0000313|Proteomes:UP000219111};
RA Varghese N., Submissions S.;
RL Submitted (AUG-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; OBMT01000005; SOC06497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285SF32; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000219111; 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}.
FT DOMAIN 11..381
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 462..497
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 520 AA; 53632 MW; A97E33D786D3A87E CRC64;
MTSHSLETHR VVIVGAGLGA LYAALKLAPH PVLVISPERL GEGASSAWAQ GGVAAAMAVS
DSPESHAKDT ETAGAGTVDA AIARLVTSDA KARILDLTTL GTPFDRDAAG GYVMSREAAH
SCPRVVRVKG DQAGHEIMET LIAEVRRSPS VQVAEGVIAS GLAVAAGRVT GVWVERADAP
SGRVLIETPA VLLAGGGSGG LFAVTTNPPR IRGQVVGMAA RAGARIADAE FVQFHPTAIA
TGEDPAPLAT EALRGEGAVL LNSRDERFMV PIHPDAELAP RDIVARAVYL EHQAGRAPAL
DTRAVLGAAL PERFPAVAEA CYQAGIDPVL KPIPVAAAAH YHMGGIAVDA RGRASIAGLW
VCGEASSTGL HGANRLASNG LLEALVFARI CAEGIAAHLP ETAAPELVLS FPGGGAGVDE
TAVTRLRAAM TDGCGVVRDA AGLARTLAII REIEAAAQSE TLLNMTATAT LIAAAALARQ
ESRGGHFRSD YPKPDPVQAE RRFLTLEEAR EIRTRALEKT
//
