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Database: UniProt
Entry: D2YH62_VIBMI
LinkDB: D2YH62_VIBMI
Original site: D2YH62_VIBMI 
ID   D2YH62_VIBMI            Unreviewed;       580 AA.
AC   D2YH62;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:EEW05919.1};
GN   ORFNames=VMB_28590 {ECO:0000313|EMBL:EEW05919.1};
OS   Vibrio mimicus VM603.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW05919.1, ECO:0000313|Proteomes:UP000004827};
RN   [1] {ECO:0000313|EMBL:EEW05919.1, ECO:0000313|Proteomes:UP000004827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VM603 {ECO:0000313|EMBL:EEW05919.1,
RC   ECO:0000313|Proteomes:UP000004827};
RX   PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA   Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA   Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT   "Genomic taxonomy of Vibrios.";
RL   BMC Evol. Biol. 9:258-258(2009).
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:EEW05919.1}.
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DR   EMBL; ACYU01000145; EEW05919.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2YH62; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000004827; 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   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   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}.
FT   DOMAIN          55..437
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          486..567
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   COILED          498..525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   580 AA;  64894 MW;  07CD6CA991F7A8D9 CRC64;
     MTFSLIGHGV DSSNARDCFT SPLPFEEFKA ISSWITHYSL GIGNFMNADR EHQCDVLVIG
     SGAAGLSLAL QVAQYGKVIV LSKGPRSEGA TFYAQGGIAA VFDESDSIES HVQDTLIAGA
     GICDEQTVRF IAEHAKECVQ WLIDGGVPFD KEDDSDTDHP RYHLTREGGH SHRRILHAAD
     ATGMAMQTSL QDNAHNHPNI TVLERHNALD LITEDKIGGD ANKIVGAYVW NRNEEHVETI
     RAKFVVLATG GASKVYQYTS NPDVSSGDGI AMAWRAGCRV ANLEFNQFHP TCLYHPEARN
     FLLTEALRGE GAYLRRPDGS RFMPDFDERA ELAPRDIVAR AIDFEMKRLG ADCMYLDISH
     KPADFIEKHF PTIYSRLMDL GIDMTKEPIP IVPAAHYTCG GVMVNPQGQT DLKQLYAIGE
     VSYTGLHGAN RMASNSLLEC VVYAWSASQD IIAQLPKASM PQSLPAWDES QVTCSDEEVV
     LQHNWHELRL FMWDYMGIVR TNKRLERAMR RIQLLQQETH EYYSNFRVSN NLLEMRNLLQ
     VAELMVRCAM QRKESRGLHY TLDYPEQLAD SGPTILVPEK
//
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