ID A0A062VQC9_9MICO Unreviewed; 500 AA.
AC A0A062VQC9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, 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 ORFNames=DC31_09110 {ECO:0000313|EMBL:KDA06548.1};
OS Microbacterium sp. CH12i.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA06548.1, ECO:0000313|Proteomes:UP000027096};
RN [1] {ECO:0000313|EMBL:KDA06548.1, ECO:0000313|Proteomes:UP000027096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH12i {ECO:0000313|EMBL:KDA06548.1,
RC ECO:0000313|Proteomes:UP000027096};
RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT shallow groundwater in Cape Hallet, Antarctica.";
RL Submitted (MAR-2014) 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 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}.
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:KDA06548.1}.
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DR EMBL; JHET01000003; KDA06548.1; -; Genomic_DNA.
DR RefSeq; WP_036277331.1; NZ_JHET01000003.1.
DR AlphaFoldDB; A0A062VQC9; -.
DR STRING; 1479651.DC31_09110; -.
DR OrthoDB; 9805351at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000027096; Unassembled WGS sequence.
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 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:UP000027096}.
FT DOMAIN 3..375
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 418..490
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 500 AA; 51380 MW; 274DCAEDCEFDA85A CRC64;
MNVIVVGSGI AGLVAALHTA EAGHTVTLLT KGALGGGSTP LAQGGVAGIY GSGDSPEAHA
ADTLSAGAGL SDPSAVNVLV SEGAERIAEL IARGVAFDRA PDGTLLLGRE AAHSHARIVH
AGGDATGAAI SSALIAQLSS CPIHVIEHAF LADLIVDDDE LTGKRAVRGV RMLCGEASVD
LEADAVILAT GGAGQLFAHT TNPLGVTGDG IAAAMRAGVA VTDLEFMQFH PTVLAAGAAF
LISEAVRGEG ATLLNDEGRR FAFDSHPDGE LAPRDVVSRA IARQAAAQGR PVLLDATMLG
ASRLAERFPT IDRVTRERGF DWAREPIPVT PAAHYLMGGI ITDLDGRTSI PGLFAVGEVA
RTGVHGANRL ASNSLLEGAV FAARAAAAVT SPFESRKLLH PRGEWHNLRD SKVPHDRSGL
QQLMWDNVGL LRTEGGLVEA LDSIRSWAAA PAPIATPRTR AEHEDASLLQ LAEAMASAAL
ARAESVGAHH IAHEPALIGA
//
