ID F7M819_9BACE Unreviewed; 624 AA.
AC F7M819;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0127_03605 {ECO:0000313|EMBL:EGM99386.1};
OS Bacteroides sp. 1_1_30.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457387 {ECO:0000313|EMBL:EGM99386.1, ECO:0000313|Proteomes:UP000004085};
RN [1] {ECO:0000313|EMBL:EGM99386.1, ECO:0000313|Proteomes:UP000004085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_30 {ECO:0000313|EMBL:EGM99386.1,
RC ECO:0000313|Proteomes:UP000004085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA 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., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. 1_1_30.";
RL Submitted (APR-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:EGM99386.1}.
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DR EMBL; ADCL01000069; EGM99386.1; -; Genomic_DNA.
DR RefSeq; WP_008644113.1; NZ_GL945099.1.
DR AlphaFoldDB; F7M819; -.
DR PATRIC; fig|457387.3.peg.3670; -.
DR HOGENOM; CLU_029779_0_0_10; -.
DR Proteomes; UP000004085; 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_5003359797"
SQ SEQUENCE 624 AA; 70171 MW; C05B70D175E807A9 CRC64;
MRNYFLGLCL FFALCFTACS 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 AALAVKEDKN IREVSVREVQ NAILDGKGYL
LPYLDVELDH PMFKSLQRIG STGILKGIGK SVDWSNQMWF RADTLLLANE LKGLGDVYPF
VNKQVFEGNN TISIQKATEL IGGIAEKEGF EMKEGRVEEI WNEFELKDFD MNRGILRSEM
AILIDQILDP FNNKKVDITG QYIQ
//