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Database: UniProt
Entry: A0A0K0Y619_9RHOB
LinkDB: A0A0K0Y619_9RHOB
Original site: A0A0K0Y619_9RHOB 
ID   A0A0K0Y619_9RHOB        Unreviewed;       522 AA.
AC   A0A0K0Y619;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN   Name=nadB_2 {ECO:0000313|EMBL:AKS46370.1};
GN   ORFNames=OSB_18290 {ECO:0000313|EMBL:AKS46370.1}, SAMN05444287_1485
GN   {ECO:0000313|EMBL:SIO12731.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS46370.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS46370.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS46370.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
RN   [2] {ECO:0000313|EMBL:SIO12731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO12731.1};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000184809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; CP012160; AKS46370.1; -; Genomic_DNA.
DR   EMBL; FSRP01000001; SIO12731.1; -; Genomic_DNA.
DR   RefSeq; WP_049834676.1; NZ_FSRP01000001.1.
DR   AlphaFoldDB; A0A0K0Y619; -.
DR   STRING; 1458307.OSB_18290; -.
DR   KEGG; otm:OSB_18290; -.
DR   PATRIC; fig|1458307.3.peg.1843; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000067444; Chromosome.
DR   Proteomes; UP000184809; 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   ECO:0000313|EMBL:AKS46370.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067444}.
FT   DOMAIN          9..380
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          461..498
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   522 AA;  54380 MW;  84572E4D2879B5D7 CRC64;
     MKTIDTDRIV IIGAGLGALY AALKLAPHPV VLISPETLGE GASSAWAQGG VAAAMDSDDS
     PVNHAEDTIS AGAGTVDPKV AKLVTQEARD HILDLTALGT PFDRTDQGGY VLSREAAHSF
     ARVVRVKGDQ AGAEIMAALI ETVRETPSIQ ALEGVMAVDL EVEDDRIIGV AVQAAHDTPS
     ASIMLRGASI LVAGGGSGGL YAQTTNPHRI RGQVIGMAAR AGAVIADPEF VQFHPTAMDV
     GEDPAPLATE ALRGEGAILI NKDGKRFMLD VHEDAELAPR DIVARAIFEQ TQAGNRPMLD
     TTTAIGAEIS EMFPSVTQAC LRNGIDPAVD PIPVAAAAHY HMGGIATDIN GKASLDGLWV
     CGEASSTGLH GANRLASNGL LEALVYARIC AEGIISTLAP VKDAPLIALT FGGGGTPPDA
     EAVQELRQTM TNCVGVVRDA KGLKTALRTI ERLEQHHGDS LSFLNMCATA TLIAAGALLR
     EESRGAHERI DFPDTRADLA QSTQLTLVDA MAYRTKICGE PA
//
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