ID A0A140NKL2_PROSM Unreviewed; 533 AA.
AC A0A140NKL2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 OrderedLocusNames=S70_03165 {ECO:0000313|EMBL:AFH92522.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH92522.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH92522.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH92522.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) 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}.
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DR EMBL; CP003488; AFH92522.1; -; Genomic_DNA.
DR RefSeq; WP_014656336.1; NC_017731.1.
DR AlphaFoldDB; A0A140NKL2; -.
DR GeneID; 79053329; -.
DR KEGG; psi:S70_03165; -.
DR PATRIC; fig|1157951.4.peg.629; -.
DR HOGENOM; CLU_014312_3_0_6; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000005012; 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; 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 10..392
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 441..521
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 533 AA; 59797 MW; 5B67EE0F7BED7311 CRC64;
MNDPTQHYTD ILIIGSGVAG LSAALRLAPF HKVTLLSKST LNEGASYYAQ GGIAAVFDNT
DSIESHVEDT LIAGAGICER EAVEFIASNA KECVQWLIDQ GVLFDTEVTE TGETQYHLTR
EGGHSHRRIL HHADATGKEV ETTLVNLAFA HPNIHVKERY NAVDLIRSDK IGLAGESRIV
GAYVWNRQKE HVETIRAKIV VLATGGAAKV YQYTTNPDIS SGDGIAMAWR IGCSVANLEF
NQFHPTCLFH PQARNFLLTE ALRGEGAYLK RPDGSRFMPD YDPRCELAPR DIVARAIDHE
MKRLGADCMY LDISHKPADF IQSHFPTIYE KLITLGLDLT KEPIPIVPAA HYTCGGVSVD
QNGMTDIPNL YAIGEVSYTG LHGANRMASN SLLECLVYGW SASQHICHAI TQIEDIPVLP
EWDDSRVHNS DEQVVIQHNW HELRLFMWDY MGIVRTTKRL ERALRRIHLL QQEIHDYYAN
FRISNNLLEL RNLVQVAELM VRCALERKES RGLHYTLDYP DLLEHSGPTV LKP
//
