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Database: UniProt
Entry: B1HY33_LYSSC
LinkDB: B1HY33_LYSSC
Original site: B1HY33_LYSSC 
ID   B1HY33_LYSSC            Unreviewed;       528 AA.
AC   B1HY33;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   OrderedLocusNames=Bsph_4289 {ECO:0000313|EMBL:ACA41748.1};
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA41748.1, ECO:0000313|Proteomes:UP000002164};
RN   [1] {ECO:0000313|EMBL:ACA41748.1, ECO:0000313|Proteomes:UP000002164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41 {ECO:0000313|EMBL:ACA41748.1,
RC   ECO:0000313|Proteomes:UP000002164};
RX   PubMed=18296527; DOI=10.1128/JB.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA41748.1; -; Genomic_DNA.
DR   RefSeq; WP_012295776.1; NC_010382.1.
DR   AlphaFoldDB; B1HY33; -.
DR   EnsemblBacteria; ACA41748; ACA41748; Bsph_4289.
DR   KEGG; lsp:Bsph_4289; -.
DR   HOGENOM; CLU_014312_3_2_9; -.
DR   OMA; HCVQWLI; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000002164; 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   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}.
FT   DOMAIN          6..371
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          413..505
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   528 AA;  58169 MW;  4F3C8F64FA11BD24 CRC64;
     MDVKTDVLII GSGIAALQAA LLLEEHFKIQ IVTKSSVHTS SSYRAQGGIA AVISEEDHID
     CHVADTLKAG EFHHESRHVQ TLIEEGTKIM RNYLKAGFPI DRHNNGAPAL GLEGAHSHHR
     ILHAGGDRTG QIFIDYLLHK LSPNTKINCY EMAYELLLNK NGDCIGVLTK GREGTKRYFA
     HHVILATGGA GALYSSTSND PTNTGDGIAL AFRAGAAISD MEFIQFHPSL LWCENEAKGL
     ISEAVRGAGG IFVDAQRRPI MKGIHAQLDL APRHITALAL FKKRAAGEET FLDISSIQNF
     DVKFPSITQL CRNNHVDLQE GLIPVSPGSH FLMGGIIADD KGRTTIANLY AIGEVACTGV
     HGANRLASNS LLEGITFGQR MAYFIIQQGC SQKDFLLAND KNVDSMPLLF SKQQLQQHMM
     QYLGIVRNGD DLQYSLQQLP SIHALLHANL KGLQQIELEL YMMHVVATLI THAAITRTET
     RGAHIRSDNP KMEAQWANRW IIFSQGQMKV RNSLYEYHQT RGNAQAIF
//
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