ID A0A1H6HU44_9EURY Unreviewed; 522 AA.
AC A0A1H6HU44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05192561_101522 {ECO:0000313|EMBL:SEH39589.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH39589.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH39589.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH39589.1,
RC ECO:0000313|Proteomes:UP000199215};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNWU01000001; SEH39589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6HU44; -.
DR STRING; 1267564.SAMN05192561_101522; -.
DR OrthoDB; 305271at2157; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000199215; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199215}.
FT DOMAIN 15..391
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 440..512
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 236..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 54565 MW; 0719617A6B7AAA30 CRC64;
MADRTDAPID GETTDLLVVG SGIAGCAAAL AGARAGANVT LATEASRPAD ATSYWAQGGI
AVTRDDPEAL KRDVIDASDG TADPAAVDVL VSGADAAVQD VLIDTLGVAF DEGYGREAAH
DEARIRHVDA ATGRHVLVPF LEHLRGLSAV EILEDTAALE LCTHEGRVHG ALLERDGEVT
PWFAGATVLA TGGIGACYPR STNPRTATGD GIAMAALAGA DVADMEYVQF HPTAFAGQGT
DERATGNETA GSGPTPDRGT FLLSEAIRGE GAVLRDATGE RFMPEYHPDA ELAPRDVVAR
AVATERERTG EVVLDVTPID FAGEFPALAS ECADRGVSLE DGIPVAPAEH FLCGGIDVDL
EGRTSLDRLY AVGECARTGV HGANRLASTS LLEGLVWGLR AGETAADTGV EAGPKPIEPP
ELLDRDPALP DRFAAEKFHR LRRVMDAELG IVRDPAGIER AQATIRRLKG EVDAYTRTRT
SRALYELRGA CVSALLITRA AAANEESRGC HQLTEGAPVD AD
//
