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Database: UniProt
Entry: T1A1G1_9ZZZZ
LinkDB: T1A1G1_9ZZZZ
Original site: T1A1G1_9ZZZZ 
ID   T1A1G1_9ZZZZ            Unreviewed;       182 AA.
AC   T1A1G1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE   Flags: Fragment;
GN   ORFNames=B1A_18182 {ECO:0000313|EMBL:EQD35655.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD35655.1};
RN   [1] {ECO:0000313|EMBL:EQD35655.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD35655.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
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:EQD35655.1}.
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DR   EMBL; AUZX01013401; EQD35655.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1A1G1; -.
DR   UniPathway; UPA00253; UER00326.
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:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; 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   SUPFAM; SSF51905; FAD/NAD(P)-binding 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}.
FT   DOMAIN          28..177
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EQD35655.1"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|EMBL:EQD35655.1"
SQ   SEQUENCE   182 AA;  19641 MW;  54317E459DC0E1F5 CRC64;
     VLEMGIEARE RTILREIRPR SSGPPETIVS AADGSGVETL DPRPLVLATG GAGSLYRQST
     NPSVTTGDGV AVAFRAGAIV SDLEFFQFHP TVFYRPGAPR FLITEALRGE GAVLRNVEGA
     RFLPSIHPDG ELAPRDVVSR AIAAEIQRTG HPCVYLDATE IPRDRIVTRF PSVCRFLATF
     GL
//
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