ID M1QCD2_9ZZZZ Unreviewed; 493 AA.
AC M1QCD2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN ORFNames=FLSS-16_0019 {ECO:0000313|EMBL:AGF93678.1};
OS uncultured organism.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=155900 {ECO:0000313|EMBL:AGF93678.1};
RN [1] {ECO:0000313|EMBL:AGF93678.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23352736; DOI=10.1016/j.syapm.2012.11.008;
RA Lopez-Lopez A., Richter M., Pena A., Tamames J., Rossello-Mora R.;
RT "New insights into the archaeal diversity of a hypersaline microbial mat
RT obtained by a metagenomic approach.";
RL Syst. Appl. Microbiol. 36:205-214(2013).
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}.
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DR EMBL; JX684102; AGF93678.1; -; Genomic_DNA.
DR AlphaFoldDB; M1QCD2; -.
DR UniPathway; UPA00253; UER00326.
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 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}.
FT DOMAIN 10..362
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 418..493
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55312 MW; 6737754542E1671D CRC64;
MITAGTNLDN GNTPQAQGGI IFNENDDSPE LLQKDIYTAG WNCNYKKAVK HISQKGSDVV
REILLDKLQI AFEKDRNGKL KLTREGGHST PRILYCADYT GRSIIDGYIK KINNSPNINV
ITNRTAVDLL TSHHQSTSLE FQYQLNNQCL GAYVFNQYTR EVETIMADFT ILATGGVGQI
FLHTTNSNSS IGSGVTMAHR SGAKTMNSEF VQFHPTALFQ RGGQQFLISE TVRGEGAKFI
RMDGKPFMKE YDSRGDLAPR DIVTRATIQE MLKTGDDFVY LDAANYISKD LPTRFPTIYN
KCLELGIDIN KDPIPVVPAA HFFCGGILVD MEGKTTLNRL YAIGECSCTG VHGANRLAST
SLLEGVLWGK QAAESIHYKI QKKNQLSKKL MESIPDWTHV GNDENEDPAL ITQDWLTIKN
TMWNYVGIVR TSSRLRRAVE DFANLSKRLY EFYRNTPISK ELIQLFHGCQ TAILITHAAR
MNKKSQGCHY RPE
//
