(data stored in ACNUC7421 zone)

SWISSPROT: E3J4U0_FRAIE

ID   E3J4U0_FRAIE            Unreviewed;       584 AA.
AC   E3J4U0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|RuleBase:RU362049};
GN   OrderedLocusNames=FraEuI1c_0171 {ECO:0000313|EMBL:ADP78259.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78259.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78259.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to
CC       iminoaspartate. {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|RuleBase:RU362049};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362049};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|RuleBase:RU362049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       NadB subfamily. {ECO:0000256|RuleBase:RU362049}.
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DR   EMBL; CP002299; ADP78259.1; -; Genomic_DNA.
DR   STRING; 298654.FraEuI1c_0171; -.
DR   EnsemblBacteria; ADP78259; ADP78259; FraEuI1c_0171.
DR   KEGG; fri:FraEuI1c_0171; -.
DR   eggNOG; ENOG4107S3R; Bacteria.
DR   eggNOG; COG0029; LUCA.
DR   HOGENOM; HOG000160476; -.
DR   KO; K00278; -.
DR   OMA; HCVQWLI; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000002484; 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; -; 1.
DR   Gene3D; 3.90.700.10; -; 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:SF2; PTHR42716:SF2; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J4U0.
DR   SWISS-2DPAGE; E3J4U0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   FAD {ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362049};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN       37    420       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      463    566       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   584 AA;  59689 MW;  80B091E440208539 CRC64;
     MTSTHLATPA APVGLPSLPV LPARLGAPRA GWTRHADVVV IGSGVAGLTA AQRVRAQLPT
     SRVLLVTKAL LDMGSTRWAQ GGIAAALAAE DSPDDHLRDT LVAGVGLCDP AAVRVLVTEG
     PARVRELAAL GARFDLTAAG ELSLTREGGH LRDRIVHAGG DATGLEVERA LIAALLADDG
     IDVIEHALVL DLLVDADGQA AGVTLHVLGE GTRDGVGAVL ARAVILATGG MGQIYASTTN
     PSVSTGDGVA LALRAGAVIA DLEFVQFHPT ALRIPGVASA GQQPLISEAM RGEGALLVDA
     AGERVMSGVH PLEDLAPRDV VAKQMSRVMG AQGVDHLFLD ARHLGEETIL RRFPTITARC
     REHGIDPVTQ PIPVAPAAHY ASGGVRTDTQ GRTSVPGLYA CGEAACTGVH GANRLASNSL
     LEGLVFAARI ADDLAGGLPS PGAPVEAVVD RGSAGLADPA ERVELERVMT EGAGVLRSAP
     SLLTTAKALA DVGDVRLTGA TVAAGPEAWE MTNLRTVATA LVAAAATRTE TRGSHWREDF
     ADADDAWRGH LLLRMDPDGL LDVTYAPAPP DGVTAGGAAE GKAP
//

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