ID G2J9H6_9BURK Unreviewed; 544 AA.
AC G2J9H6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=nadB {ECO:0000313|EMBL:CCD29423.1};
GN ORFNames=CAGGBEG34_230066 {ECO:0000313|EMBL:CCD29423.1};
OS Candidatus Glomeribacter gigasporarum BEG34.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Glomeribacter.
OX NCBI_TaxID=1070319 {ECO:0000313|EMBL:CCD29423.1, ECO:0000313|Proteomes:UP000054051};
RN [1] {ECO:0000313|EMBL:CCD29423.1, ECO:0000313|Proteomes:UP000054051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEG34 {ECO:0000313|EMBL:CCD29423.1,
RC ECO:0000313|Proteomes:UP000054051};
RA Ghignone S., Salvioli A., Anca I., Lumini E., Ortu G., Petiti L.,
RA Cruveiller S., Bianciotto V., Piffanelli P., Lanfranco L., Bonfante P.;
RT "The genome of the obligate endobacterium of an arbuscular mycorrhizal
RT fungus reveals an interphylum network of nutritional interactions.";
RL Submitted (AUG-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCD29423.1}.
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DR EMBL; CAFB01000040; CCD29423.1; -; Genomic_DNA.
DR RefSeq; WP_006682614.1; NZ_CAFB01000040.1.
DR AlphaFoldDB; G2J9H6; -.
DR STRING; 1070319.CAGGBEG34_230066; -.
DR eggNOG; COG0029; Bacteria.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000054051; Unassembled WGS sequence.
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:UP000054051}.
FT DOMAIN 4..383
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 433..514
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 445..472
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 544 AA; 59810 MW; 92FFCADD3C3E2346 CRC64;
MEFDVLIAGS GLAGLSAALS LAESRRVAVL TKRGATDGAS DWAQGGIAVS LDASDSAERH
MEDTCAAGCA LCDAAAVRFV IEHSRSAVEW LMARGAPFTR DAQAASGFHL TREGGHRQRR
ILHAADATGH AVMTLLAEQA QAHPNITLFD AHFAIDLIHS ARLGLSGQRC YGLYALDMRT
GSVRTFRARH TILATGGAGK AYLYTTNPDT ATGDGMAMAW RAGCRIANME FIQFHPTCLY
HPYAKSFLIS EAVRGEGGVL KLPDGARFMP AYDARAELAP RDIVARAIDF EIKKRGMDCV
YLDIHHRPAE FLRAHFPTIL ARCLEFGIDI TREPIPVVPA AHYACGGVVT DVYGRADLAG
LYAIGETACT GLHGANRLAS NSLLECVVMG RAAAQAILAA SEKERHEIPA LPAWDESRVT
DSDEEVVITH NWDELRRLMW NYVGIVRTDK RLARAAHRIV RLREEIDEYY AHFRISRDLL
ELRNLVDVAS LIVESARFRH ESRGLHFNRD WPEMQPKGLP TILSRAFSSR VTTGASAKRH
RENH
//
