ID   C3QC46_9BACE            Unreviewed;       624 AA.
AC   C3QC46;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=FAD dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BSAG_01241 {ECO:0000313|EMBL:EEO49530.1};
OS   Bacteroides sp. D1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO49530.1, ECO:0000313|Proteomes:UP000003361};
RN   [1] {ECO:0000313|EMBL:EEO49530.1, ECO:0000313|Proteomes:UP000003361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:EEO49530.1,
RC   ECO:0000313|Proteomes:UP000003361};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA   White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEO49530.1}.
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DR   EMBL; ACAB02000110; EEO49530.1; -; Genomic_DNA.
DR   RefSeq; WP_004313256.1; NZ_JH114350.1.
DR   AlphaFoldDB; C3QC46; -.
DR   HOGENOM; CLU_029779_0_0_10; -.
DR   Proteomes; UP000003361; 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   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR005288; NadB.
DR   PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR   PANTHER; PTHR42716:SF3; SLL1913 PROTEIN; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..624
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002929065"
SQ   SEQUENCE   624 AA;  70097 MW;  44E95609D0077392 CRC64;
     MRNYFLGLCL LFALCFTACS HSDDSVDVLI IGGGASGVTA GIQSARMGAA TLIVEETEWL
     GGMLTSAGVS AVDGNYDLPA GLFGEFRGHL ADYYGGLDSL KTGWVSAVLF EPSVGNKIFH
     EMVDAEKNLK VWHNATLVKL ERENDAWIAQ IQMKDNTIKK IHAKILIDGT ELGDIAKMCG
     VKYDVGMESR HDTKEDIAPE EKNNIVQDIT YVAILKDYGK DVTIPCPEGY NKDEFACACA
     SHVCITPKEP DRVWSKDMMI TYGKLPNNKY MINWPIEGND YYVNLIEMTR EEREEALKYA
     KHYTMCFVYF LQHELGFNTL GLADDEYPTA DKLPFIPYHR ESRRIHGLVR FDLNHACEPF
     RQSQPLYRTC IAVGNYPVDH HHTRYHGYEE LPNLYFHPIP SYGLPLGTLI PKDVEGLIVA
     EKSISVSNII NGTTRLQPMV MQIGQAAGAL AALAVKEGKN MREVSVREVQ NAILDGKGYL
     LPYLDVELDH PMFKSLQRIG STGILKGIGK SVDWSNQMWF RADTLLLANE LKGLGDVYPF
     VNKQVFEGNN TISIQKATEL IGGIAEKEGF EMKEGRVEEI WNEFELKDFD MNRGILRSEM
     AILIDQILDP FNNKKVDITG QYIQ
//