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Database: UniProt
Entry: A0A0M3UBI7_9PSEU
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ID   A0A0M3UBI7_9PSEU        Unreviewed;       533 AA.
AC   A0A0M3UBI7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   ORFNames=XF36_15545 {ECO:0000313|EMBL:ALE84385.1};
OS   Pseudonocardia sp. HH130629-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE84385.1, ECO:0000313|Proteomes:UP000062082};
RN   [1] {ECO:0000313|EMBL:ALE84385.1, ECO:0000313|Proteomes:UP000062082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE84385.1,
RC   ECO:0000313|Proteomes:UP000062082};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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         ECO:0000256|RuleBase:RU362049};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004950, ECO:0000256|RuleBase:RU362049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC       subfamily. {ECO:0000256|ARBA:ARBA00008562,
CC       ECO:0000256|RuleBase:RU362049}.
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DR   EMBL; CP011868; ALE84385.1; -; Genomic_DNA.
DR   RefSeq; WP_060712551.1; NZ_CP011868.1.
DR   AlphaFoldDB; A0A0M3UBI7; -.
DR   KEGG; pseh:XF36_15545; -.
DR   PATRIC; fig|1641402.3.peg.3325; -.
DR   OrthoDB; 9805351at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000062082; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-UniRule.
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   GO; GO:0008202; P:steroid metabolic process; IEA:UniProt.
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   NCBIfam; TIGR00551; nadB; 1.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362049};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU362049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062082}.
FT   DOMAIN          13..388
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          431..506
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   533 AA;  53370 MW;  9E14E21500C38017 CRC64;
     MTARGAGWEA GADLVVVGSG VAGLTAALDA AAAGLRVVVV TKDGIGEGST RWAQGGVAVV
     LGDIAGDTPD SHVADTVAAG GGLNDVAAVE TIVRAGPDAV RRLRARGALF DLSGDRPART
     REGGHSAYRV VHAGGDATGA EIERALVAAT RSAQLTVLDG HVAADLLRDA GRVTGLTVLD
     ADGRAGVLSA PAVLLATGGY GQLYATTTNP ATSTGDGVAL ALRAGAVAAD LEFVQFHPTV
     LWTGPGSGTA GRRPLVTEAV RGEGAVLRDR AGTAFMAGVH PRADLAPRDV VAAAITRRMA
     ETGSECAWLD ATAFDGFAAR FPTVYASCRA AGIDPLTEPI PVTPAAHYAC GGVVTDTSGR
     TGVPGLYAAG EVARTGLHGA NRLASNSLLE GLVVGERVVR AVLADAGPTG VPAPAVTVPA
     LPVADRTVVQ RAMSGSAGIG RDAAGLAGAS DAIEAVTTTA VPVDRTGVED AALTLIAQAV
     LVAAGTRRET RGCHVRTDFP DRDDTHQRSS LRIRVDATGR PVVVADGSLV GAA
//
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