GenomeNet

Database: UniProt
Entry: A0A1I3EGR2_9BRAD
LinkDB: A0A1I3EGR2_9BRAD
Original site: A0A1I3EGR2_9BRAD 
ID   A0A1I3EGR2_9BRAD        Unreviewed;       535 AA.
AC   A0A1I3EGR2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=SAMN05216525_103174 {ECO:0000313|EMBL:SFH98053.1};
OS   Bradyrhizobium sp. Gha.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFH98053.1, ECO:0000313|Proteomes:UP000199284};
RN   [1] {ECO:0000313|EMBL:SFH98053.1, ECO:0000313|Proteomes:UP000199284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gha {ECO:0000313|EMBL:SFH98053.1,
RC   ECO:0000313|Proteomes:UP000199284};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOQM01000003; SFH98053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3EGR2; -.
DR   STRING; 1855318.SAMN05216525_103174; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000199284; 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   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, 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}.
FT   DOMAIN          15..386
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          429..498
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   535 AA;  54387 MW;  D3C58B43673663DE CRC64;
     MTYNIHNLTR SVDEVVIVGG GLAGLFCALK LAPRPVTLIA AAPLGQGASS AWAQGGIAAA
     VAEGDGPEAH AADTIAVGGG IVDEAIALGI AREAGSRIHD LLAYGVPFDR DLEGRLAVGR
     EAAHSARRIV HVRGDAAGAA IIAALSEAAR RTPSIRLIEG FVAEALLTED GAVTGLQLRE
     AGSCAAMPIM IASRAVVLAT GGIGHLYAVT TNPAQASGSG LAIAARAGAV IADTEFVQFH
     PTAIMVGRDP APLATEALRG EGATLINGNG ERFMAAQHPL AELAPRDIVA RGVFAEIAAG
     RGAFLDARQA LGMHFAEKFP TVHASCIAAG IDPAIEAIPI APAVHYHMGG IAVDARGRSS
     IDGLWAGGEV ASTGAHGANR LASNSLLEAV VYAARIADDI AGHTMPSPSR LPEALLTPRG
     GAPDAAAVKR LRTMMSANVG VIRDGDGLAE AVRSMAALEH SANSVAVRNM ATAALLVATA
     AWSRRESRGA HFRSDHPADV PALAQRTMTT LAAARAIADG LADPSTPRLA QSMIA
//
DBGET integrated database retrieval system