ID M5E0X2_9GAMM Unreviewed; 535 AA.
AC M5E0X2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 ORFNames=TOL_0913 {ECO:0000313|EMBL:CCU71349.1};
OS Thalassolituus oleivorans MIL-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU71349.1, ECO:0000313|Proteomes:UP000011866};
RN [1] {ECO:0000313|EMBL:CCU71349.1, ECO:0000313|Proteomes:UP000011866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU71349.1,
RC ECO:0000313|Proteomes:UP000011866};
RX PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA Yakimov M.M., Teeling H., Golyshina O.V.;
RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL Genome Announc. 1:1-3(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 ---------------------------------------------------------------------------
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; HF680312; CCU71349.1; -; Genomic_DNA.
DR RefSeq; WP_015486086.1; NC_020888.1.
DR AlphaFoldDB; M5E0X2; -.
DR STRING; 187493.CN03_13625; -.
DR KEGG; tol:TOL_0913; -.
DR PATRIC; fig|1298593.3.peg.881; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_0_6; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000011866; 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:UP000011866}.
FT DOMAIN 8..385
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 434..514
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 535 AA; 58887 MW; D1EFAB78A25DE05A CRC64;
MSQSFTYDVL IIGSGAAGLT LGLSLPEHIK AAIISKDSLD AGSTRWAQGG VAAVLDDEDS
IDAHVEDTLI AGAGLCHEPA VRYTVEESTA AIEWLIDIGV PFTQDSPNHF HLTREGGHSA
RRIIHAADAT GHAISDTLLE RARNCQNLTL LQDHIAIDLV TRSKLGLPGQ ACVGGYFLNN
ETGDVDVITA RAVVLATGGA SKVYLYTSNP DGASGDGIAM AWRAGCRVAN MEFNQFHPTC
LYHPQAKSFL ITEAVRGEGG KLLLPNGKRF MQHFDERAEL APRDIVARAI DHEMKRLGAD
CLFLDISHKP ADFIKEHFPT IYERCLQLNI DITKDPIPVV PAAHYTCGGV VTDIHGRTDI
ERLYAVGETA STGLHGANRL ASNSLLECLV FARSAAKHIA ENLDLAASVE KVPAWDSSQV
TDSDEDVVIA HNWDELRRFM WDYVGIVRTT KRLLRAKHRV KLLRQEIQEF YSNHKVTNDL
LELRNLVDVA DVIIRSALLR KESRGLHFSR DYPEPLPRAF DTVLTPKYIK ELGEL
//
