ID   E0I728_9BACL            Unreviewed;       557 AA.
AC   E0I728;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EFM11844.1};
GN   ORFNames=PaecuDRAFT_1452 {ECO:0000313|EMBL:EFM11844.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11844.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM11844.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM11844.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; AEDD01000003; EFM11844.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0I728; -.
DR   STRING; 717606.PaecuDRAFT_1452; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000005387; Unassembled WGS sequence.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
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   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   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.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT   DOMAIN          14..220
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          428..512
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   557 AA;  60352 MW;  E36C643568074C13 CRC64;
     MKREHELEEK FIADVLVLGG GPAGAWAAWR AASEGAKVIL ADKGYVGTSG ATAPGGTTLL
     VIPPIAELRE QAVAARLKAG GYLSENAWIH RVLDQVDINL QLLEQWGYPF RQDEQGHTLR
     THLHGPEYMQ LMRRVIRKLG VRILDQSPAL ELLADEYGVG GARGVNRLTG KSWEVRAHAV
     IMATGGCTFL SKGLGCNVLT GEGLLMASEA GAELSGMEFS RQYAPSFADG SVTRGRMLAW
     STLYDEHGNA LHQGDRTFGS LQKLLLDGPV YASIDLADTP EKQTFLRKAH PIFFMPLERA
     GINPFTDKFP LTLRYEGTMR GTGGLRLIGE ECATSVAGLY AAGDAASREK VTGAVSGGGA
     YNASWAICSG TWAGSGAALY ALNQKRDAGS RSLRSVGRYG LAAGQASSER LETKPLIEAI
     QREVLPLEIN YFRSEPVIRA SLDRLHKLKA ALEGRIVDDA TVQGKVRARE TAGMLTVARW
     MYTAALARKE TRGLQSLAEY PQLDPRQTHR LIVSGIEDIR IRAEKVPHAQ ECLAAIAPQS
     EVSRGSKPIA RKEELLT
//