ID M0FD57_9EURY Unreviewed; 534 AA.
AC M0FD57;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE AltName: Full=Quinolinate synthase B {ECO:0000256|ARBA:ARBA00030386};
GN ORFNames=C467_07105 {ECO:0000313|EMBL:ELZ57172.1};
OS Halorubrum hochstenium ATCC 700873.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ57172.1, ECO:0000313|Proteomes:UP000011689};
RN [1] {ECO:0000313|EMBL:ELZ57172.1, ECO:0000313|Proteomes:UP000011689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ57172.1,
RC ECO:0000313|Proteomes:UP000011689};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562}.
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:ELZ57172.1}.
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DR EMBL; AOJO01000033; ELZ57172.1; -; Genomic_DNA.
DR RefSeq; WP_008583406.1; NZ_AOJO01000033.1.
DR AlphaFoldDB; M0FD57; -.
DR STRING; 1227481.C467_07105; -.
DR GeneID; 72714167; -.
DR PATRIC; fig|1227481.4.peg.1408; -.
DR OrthoDB; 305271at2157; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000011689; Unassembled WGS sequence.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
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 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 PRINTS; PR00411; PNDRDTASEI.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000011689}.
FT DOMAIN 8..398
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 446..528
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 513..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 55794 MW; 3036E1737577A956 CRC64;
MTGHETADVL VVGSGIAGLA AALAAAREGR EVLVATKAAR PEDASSWWAQ GGIAVARDHP
DRFRRDILAA SDGTADPEAV DVLVENANDA VRDVLVETLG VAFDGEADAS AGADASAGAG
GSGTAAAFAD RGDGGFDFGR EAAHTEDRIL HVGAETGKHV HVPLLNHLDD RAGVEVRTDA
AALELIGHEG RIHGAVVESD GDRIPVYADA TVLATGGVGD LFARSTNPAG ATGDGVAMAA
LAGATVTDAE FVQFHPTAYA AGPDEDGFLV SEAVRGEGAL LRNGDGERFM PDYHPDAELA
PRDVVARAVD REREATGSVV LDVGPLDFAD EFPGLAAKCE DRGVDWSRGI PVAPAEHFLC
GGVDVDDRGR TDLDRLYAVG ECARTGVHGA NRLASTSLLE GLVWGLRAGA DAADAAVDAD
PEAVETPDLL DRDPALPDDF ARQKFRRLRR VMDECAGIER DADDLNRALG VLRRLKGEVD
AYVRTRTSRS LYELRNATVT ALLVTRQALA NEESVGTHYR TDAAEPADPG PADD
//
