ID Q5YQI0_NOCFA Unreviewed; 554 AA.
AC Q5YQI0;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=L-aspartate oxidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=NFA_47100 {ECO:0000313|EMBL:BAD59561.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59561.1, ECO:0000313|Proteomes:UP000006820};
RN [1] {ECO:0000313|EMBL:BAD59561.1, ECO:0000313|Proteomes:UP000006820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59561.1,
RC ECO:0000313|Proteomes:UP000006820};
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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};
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DR EMBL; AP006618; BAD59561.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YQI0; -.
DR STRING; 247156.NFA_47100; -.
DR KEGG; nfa:NFA_47100; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_5_11; -.
DR Proteomes; UP000006820; Chromosome.
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 Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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 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; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006820}.
FT DOMAIN 19..226
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 455..494
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 514..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 57039 MW; 838968975B3D0022 CRC64;
MRPGELWPNI SIMTDIETDV LVLGGGPAGI WAALSAAASG AAVVLVDKAW CAGSGPAAEG
VHTLWNLPPG PGREEAVRRT LLHGGGLGDP TWMHRVLDET YRRTTELTRW GYRVPGARRS
ATPALAYLDG ARHLRLLRRT LRLLGVRVLD RHPALHLLTD RDGVVAGAAG VRTGDRCLPW
TARAGAVVLA TGGCAFGSGA AGTAGATGEG LLMAAEAGAR LSGMEFSCGY GLAVAAHPAG
PVLRSARALQ PALRSATLVD EDGAPLAGHR SAALAALADG RRVYALPAGL LVATRARLER
LGLIDAAGRV PVRAVLEGTV RGTGGLRLTG ADCATTVAGL YAAGDVADRE QISGAASGSG
GHHAAWAIAS GAWAGAAAAG YARRRGIPAA AFPVPGAGLA TRANLDPRAV VGLVQEHTLP
LRRSYLRSAD SLRDSIAELD ALWPGARFEL GGYGHGRVSA REAAALLAVA RWADHAALAR
TESRGMHRRA DHPGAAPDWR VRLLVGGLDE IRVERERPPA ARETGRGRGS TTPRSARVRG
SSGPGLTPGG AVPL
//
