ID A0A1C7D6B3_9SPHN Unreviewed; 528 AA.
AC A0A1C7D6B3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:ANU06994.1};
GN ORFNames=A6F65_00672 {ECO:0000313|EMBL:ANU06994.1};
OS Paraurantiacibacter namhicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Paraurantiacibacter.
OX NCBI_TaxID=645517 {ECO:0000313|EMBL:ANU06994.1, ECO:0000313|Proteomes:UP000092698};
RN [1] {ECO:0000313|EMBL:ANU06994.1, ECO:0000313|Proteomes:UP000092698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16345 {ECO:0000313|EMBL:ANU06994.1,
RC ECO:0000313|Proteomes:UP000092698};
RA Cheng H., Wu Y.-H., Jian S.-L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT "Complete genome sequence of Altererythrobacter namhicola JCM 16345T,
RT containing esterase-encoding genes.";
RL Submitted (JUL-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; CP016545; ANU06994.1; -; Genomic_DNA.
DR RefSeq; WP_067789905.1; NZ_CP016545.1.
DR AlphaFoldDB; A0A1C7D6B3; -.
DR STRING; 645517.A6F65_00672; -.
DR KEGG; anh:A6F65_00672; -.
DR PATRIC; fig|645517.4.peg.674; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000092698; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092698}.
FT DOMAIN 7..387
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 437..519
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 528 AA; 58318 MW; 40D315AC8E179296 CRC64;
MDTHEHDVLI IGSGAAGLSA ALELATQRSV LVLAKGALNS GSTAWAQGGI AAVLDAGDTF
ENHIRDTMVA GAGLNDRDTV EFVIENAPQA IDRLCELGVP FNREDNDLHL TREGGHSHRR
IVHVDDATGW AVQAALLKAA EENPNITLLP DQTCIDLITG RNAEKYSGDG RVWGAYALDT
KSGKVAAHVA RATVLAAGGA GRVYQFSTAP RGATGDGIAM AWRAGARVSN MEMMQFHPTC
LYNLEVKNFL ITEAVRGEGG RLFNPVTGER YMEQYDAERM ELAPRDIVAR ANDDQIKRHG
LDYVHLDISH QPPEFVKEHF PTIHEKLLGL GIDMTKEPIP VVPAQHYTCG GVIIGLDART
DLPGLWAAGE CTESGLHGAN RLASNSLLEC FVFGEAAGRD ILECWDKLDD PPAIREWDDT
RVTDSDEEVV IKQNWTEIRR FMWNYVGIVR TTKRLERARH RIAMLGREIE DYYGSFRVTT
DLIELRNLHQ SAYLIVESAL KRHESRGLHF TLNYPETDEV ARDTVLVP
//
