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Database: UniProt
Entry: U2E310_9GAMM
LinkDB: U2E310_9GAMM
Original site: U2E310_9GAMM 
ID   U2E310_9GAMM            Unreviewed;       553 AA.
AC   U2E310;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   Name=nadB {ECO:0000313|EMBL:ERJ18276.1};
GN   ORFNames=SSPSH_002904 {ECO:0000313|EMBL:ERJ18276.1};
OS   Salinisphaera shabanensis E1L3A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Salinisphaera.
OX   NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18276.1, ECO:0000313|Proteomes:UP000006242};
RN   [1] {ECO:0000313|EMBL:ERJ18276.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18276.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=21705588; DOI=10.1128/JB.05459-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT   the harsh, variable environment of the brine-seawater interface of the
RT   Shaban Deep in the Red Sea.";
RL   J. Bacteriol. 193:4555-4556(2011).
RN   [2] {ECO:0000313|EMBL:ERJ18276.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18276.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
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:ERJ18276.1}.
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DR   EMBL; AFNV02000021; ERJ18276.1; -; Genomic_DNA.
DR   RefSeq; WP_021031790.1; NZ_AFNV02000021.1.
DR   AlphaFoldDB; U2E310; -.
DR   STRING; 1033802.SSPSH_002904; -.
DR   eggNOG; COG0029; Bacteria.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000006242; 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; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
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:UP000006242}.
FT   DOMAIN          13..397
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          446..529
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   553 AA;  60381 MW;  2D8C4CCB529E0B0A CRC64;
     MQSTDPQVCK RFDVVVVGSG AAGLTLALRL ARSGRRIAVI SKGALAEGST LYAQGGISAV
     LDAGDSVEAH VADTLAAGAG LCDEAAVRHT VSHSREAIEW LIERGVPFTR ADESDAESGY
     AYHLNREGGH SHRRIIHADD ATGRAVETTL EGLTRASEQI TIFEHHMAVE LIVMADAYEP
     SGRCRGVYVL DIEADTVHTF AADQVVLATG GANLAYLYSS NPHAASGDGI AMAWRAGARV
     ANMEFMQFHP TCLYHPKAHS FLISEALRGE GAVLRLADGS RFMPRHDERA ELAPRDVVAR
     AIDAEMKRTG QPHVWLDITH AGKAFIEKHF PAINARCLEL GLDMSVEPLP VVPAAHYTCG
     GVITDLAGRT DIAGVYAIGE CAFTGLHGAN RMASNSLLEC IVYASSAAAD IEARNDRVES
     AVALPAWDES RVTDSDEEVV VAHNWQELRR FMWDYVGIVR TTKRLERALH RIELLRREIH
     DYYGSFRVTP GLLELRNLAQ VAELIIRSAL DRRESRGLHF ISDFPHTLPR AMHTVLSPER
     SREIGPGVAY RPL
//
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