(data stored in SCRATCH zone)

SWISSPROT: A8LCM6_FRASN

ID   A8LCM6_FRASN            Unreviewed;       598 AA.
AC   A8LCM6;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|RuleBase:RU362049};
GN   OrderedLocusNames=Franean1_0198 {ECO:0000313|EMBL:ABW09665.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09665.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW09665.1; -; Genomic_DNA.
DR   RefSeq; WP_012157642.1; NC_009921.1.
DR   STRING; 298653.Franean1_0198; -.
DR   EnsemblBacteria; ABW09665; ABW09665; Franean1_0198.
DR   KEGG; fre:Franean1_0198; -.
DR   eggNOG; ENOG4108IYU; Bacteria.
DR   eggNOG; COG0029; LUCA.
DR   HOGENOM; HOG000160476; -.
DR   KO; K00278; -.
DR   OMA; HCVQWLI; -.
DR   OrthoDB; 153138at2; -.
DR   BioCyc; FSP298653:G1G9X-194-MONOMER; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000001313; 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; A8LCM6.
DR   SWISS-2DPAGE; A8LCM6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   FAD {ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362049,
KW   ECO:0000313|EMBL:ABW09665.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   DOMAIN       20    402       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      452    557       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   598 AA;  61757 MW;  1AC4912C30A5E2B4 CRC64;
     MPVLPHRLGA PRPGWTRHAD IVVIGSGVAG LTTVLHARAA SPDSRVLLVT KALLDAGSTR
     WAQGGIAAAL GVGDSPAEHH RDTLVAGVGL CDPVAVDILV TEGPARVREL AALGARFDRE
     PDGALSLTRE GGHLRDRIAH AGGDATGLEV ERALIAAVRA DPSIEVLEHA LVLDLLTDRG
     GRAVGATLHV LGEGSRDGVG AVTARAIVLA TGGMGQIFAS TTNPAVSTGD GVALALRAGA
     VVTDLEFVQF HPTALWLPEH ESGQQPLVSE AMRGEGALLV DAAGRRVMAG VHPLADLAPR
     DVVAKRMSRV MAEQGVRHLF LDARHLGTET LLRRFPTITA RCRAAGIDPV TMPIPVAPAA
     HYASGGVRTD VWGRTSVPGL YACGEVACTG VHGANRLASN SLLEGLVFAA RIAEHIAGLP
     GVRPVDGPGG TPSTGEPTGA RGSGLTDPTE RGDLARVMTD GAGVLRSAES LRATSKMLAG
     LGDLRVSGAT VQAGPAAWEM TNLRTVATAL VAAAELRTET RGCHWREDFG ARDDEHWRGH
     VLTRLDQEGK LIVTYEAPPA EERSNGARAA QGPSARSQAP SAPSAPSGRS AASQARSA
//

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