ID W9GUJ9_9MICO Unreviewed; 427 AA.
AC W9GUJ9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE Flags: Fragment;
GN ORFNames=N864_04115 {ECO:0000313|EMBL:EWT07524.1};
OS Intrasporangium chromatireducens Q5-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT07524.1, ECO:0000313|Proteomes:UP000019494};
RN [1] {ECO:0000313|Proteomes:UP000019494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC first step in the de novo biosynthesis of NAD(+).
CC {ECO:0000256|ARBA:ARBA00029426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
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:EWT07524.1}.
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DR EMBL; AWQS01000010; EWT07524.1; -; Genomic_DNA.
DR RefSeq; WP_034713073.1; NZ_AWQS01000010.1.
DR AlphaFoldDB; W9GUJ9; -.
DR OrthoDB; 9805351at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000019494; 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:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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; 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; 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 PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding 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:UP000019494}.
FT DOMAIN 19..401
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:EWT07524.1"
SQ SEQUENCE 427 AA; 43026 MW; 1AAF72C813DB6770 CRC64;
MTLSQLSPAG AAGATGVPVI VGAGLAGLVT ALRLAPHPVI VLAAGRLGHG AASGWAQGGI
AAALGDDDSA QLHAADTIAA GAGLCEPEVV ARITAAAPAA VDYLAELGAR FDRTPDGRYR
LGLEGAHSRR RIVHAAGDGT GAEVLRAVVG AVRRTPSITV LEGTIATRLL VADGRVAGVA
AERAAWSPAP ALLATPAHAA PGALASRSFQ LRSERVILAT GGSGQLWRHT TNPTGSRGQG
LALAARAGAE LRDLEMVQFH PTALDVGLDP MPLVSEAVRG AGALLVDATG APLTDDPLAA
RDVVARAVWG ELSRGGRVFL DARGALGSRF ADAFPTVARA CQAAGIDPAT DLIPVRPAAH
YQCGGVTVDR HGRTTVPGLW AVGEVASTGL HGANRLASNS LLEAVVCGGW VADDLANDLP
SKGHQPT
//
