ID K6V5U0_9MICO Unreviewed; 516 AA.
AC K6V5U0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN Name=nadB {ECO:0000313|EMBL:GAB77573.1};
GN ORFNames=AUCHE_05_04860 {ECO:0000313|EMBL:GAB77573.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77573.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB77573.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77573.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-2012) 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:GAB77573.1}.
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DR EMBL; BAGZ01000005; GAB77573.1; -; Genomic_DNA.
DR RefSeq; WP_006502325.1; NZ_BAGZ01000005.1.
DR AlphaFoldDB; K6V5U0; -.
DR STRING; 100225.SAMN05421595_1411; -.
DR eggNOG; COG0029; Bacteria.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000008495; 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; 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 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:UP000008495}.
FT DOMAIN 8..369
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 462..486
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 391..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 53641 MW; 1A596C83A9E8C21C CRC64;
MMSTAPAAVI VGSGLAGLVT ALELARPCVV VTAGTFASEC SSDLAQGGIA AVVGPDDDID
LHVQDTLTAG AGLCEPDVVR RIVSCGPQVV DYLQRLGVPF DRSPDGMLIL GLEGAHCRRR
IVHVDGDSTG HAVTAAVARA VRTAPWITVL EHTRARRLLW DTDGVVDGVV VEGAASGTIP
AGQIVLATGG IGGLFARTTN PRASWGSGLA LGLRAGALAQ DLEMVQFHPT ALAVGTDPMP
LVSEAVRGDG ARLIDERGRH LLEDDLAPRD IVSRAVADRL DQGGTVYLDT PAAYGESFSR
RFPTVAAQCA AAGLDPATAP LPVCPAAHYH MGGLAVDGDG RTTVPGLWAV GEVAATGLHG
ANRLASNSLL EAVVTARATA SALRARIDLD TRRRSSPSAS RTSRFVLHEG SGPESSRCGR
SGPDEEMRRL MDRHCGVLRD EQRLHTALSS LGPGALHDDA HLVALMILWS ALSRTESRGA
HRRIDCSGSG APAHTLFTAA EVLARIEVAA AQNRSA
//
