ID A0A0K2AVR3_STRA7 Unreviewed; 577 AA.
AC A0A0K2AVR3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 Name=nadB {ECO:0000313|EMBL:AKZ57225.1};
GN ORFNames=SAM23877_4180 {ECO:0000313|EMBL:AKZ57225.1};
OS Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS NBRC 12836 / NRRL B-2516).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=278992 {ECO:0000313|EMBL:AKZ57225.1, ECO:0000313|Proteomes:UP000061018};
RN [1] {ECO:0000313|Proteomes:UP000061018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL
RC B-2516 {ECO:0000313|Proteomes:UP000061018};
RX PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA Leblond P.;
RT "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT spiramycin producer.";
RL J. Biotechnol. 214:117-118(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; CP012382; AKZ57225.1; -; Genomic_DNA.
DR RefSeq; WP_053134912.1; NZ_CP012382.1.
DR AlphaFoldDB; A0A0K2AVR3; -.
DR STRING; 1889.SAM40697_3754; -.
DR KEGG; samb:SAM23877_4180; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000061018; 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 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 PIRSF; PIRSF000171; SDHA_APRA_LASPO; 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:UP000061018}.
FT DOMAIN 20..399
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 447..559
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 551..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 577 AA; 60637 MW; 37093BF0CFEFF65A CRC64;
MTSTGIRLHA PAPGWAIAAD VVVVGSGVAG LTAALRCEAA GLRTVVVTKA RLDDGSTRWA
QGGIAAALGE GDTPEQHLDD TLVAGAGLCD EEAVRTLVTE GPDAVRRLIA TGAHFDESTE
GGLALTREGG HHRRRIAHAG GDATGAEISR ALVEAVRARG MRTIENALVL DLLTDAGGRT
AGVTLHVMGE GQHDGVGAVH APAVVLATGG MGQVFSATTN PSVSTGDGVA LALRAGAEVS
DLEFVQFHPT VLFLGPDAEG QQPLVSEAVR GEGAHLVDAD GVRFMLGQHE LAELAPRDIV
AKGIMRRMQE RGTEHMYLDA RHFGAAMWEH RFPTILAACR AHGIDPVTEP IPVAPAAHYA
SGGVRTDAHG RTTVAGLYAC GEVACTGVHG ANRLASNSLL EGLVYAERIA ADIAASHAAD
TLPAPAPAPL PQPAHPAHPL LPPEARLTVQ RIMTGGAGVL RSADSLARAA DQLHHLHTEA
REALYENGKT SEPGVDTWEA TNLLCVARVL VAAAQRREET RGCHWREDHA DRDDTTWRRH
IVVRLNPDRT LAVHTTETAD FPPTTDSPQS PQRPQEQ
//
