UniProt: A0A1S2KTW3

Database: UniProt
Entry: A0A1S2KTW3_9BACI

LinkDB:  A0A1S2KTW3_9BACI 
Original site:  A0A1S2KTW3_9BACI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (8)   
   InterPro (6)   
   Pfam (2)   
Literature (2)   
   PubMed (2)   
All databases (19)   

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ID   A0A1S2KTW3_9BACI        Unreviewed;       525 AA.
AC   A0A1S2KTW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:QOY36333.1};
GN   ORFNames=AWH56_001140 {ECO:0000313|EMBL:QOY36333.1}, AWH56_24400
GN   {ECO:0000313|EMBL:OIJ03608.1};
OS   Anaerobacillus isosaccharinicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX   NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ03608.1, ECO:0000313|Proteomes:UP000180175};
RN   [1] {ECO:0000313|EMBL:OIJ03608.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:OIJ03608.1,
RC   ECO:0000313|Proteomes:UP000180175};
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT   Anaerobacillus genus.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QOY36333.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY36333.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=28104661;
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT   Anaerobacillus Genus.";
RL   Genome Announc. 5:e01493-16(2017).
RN   [3] {ECO:0000313|EMBL:QOY36333.1, ECO:0000313|Proteomes:UP000180175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY36333.1,
RC   ECO:0000313|Proteomes:UP000180175};
RX   PubMed=29580368;
RA   Bassil N.M., Lloyd J.R.;
RT   "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT   degrades isosaccharinic acid.";
RL   Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN   [4] {ECO:0000313|EMBL:QOY36333.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NB2006 {ECO:0000313|EMBL:QOY36333.1};
RA   Bassil N.M., Lloyd J.R.;
RL   Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CC       {ECO:0000256|RuleBase:RU362049}.
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; LQXD01000210; OIJ03608.1; -; Genomic_DNA.
DR   EMBL; CP063356; QOY36333.1; -; Genomic_DNA.
DR   RefSeq; WP_071319515.1; NZ_CP063356.1.
DR   AlphaFoldDB; A0A1S2KTW3; -.
DR   KEGG; aia:AWH56_001140; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000180175; Chromosome.
DR   Proteomes; UP000180175; 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: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   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:UP000180175}.
FT   DOMAIN          7..372
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          415..503
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   525 AA;  58142 MW;  1B11F6910D12EC5F CRC64;
     MNVKKTDVVI IGGGLAGLMT ADYLCNDRNV MLITKSELNH SNSWLAQGGI AAAMTKEDHW
     QEHFNDTIVA GGFHNNRETT EILVKHGTRL IKKLIEMGVS FDKDDNNQLS LGMEGAHGKR
     RILHAGGDAT GKVVVEAIMA RVLSKIEVFE QEMAYDLLVE NGVCLGVFTK DTNEDIWFIE
     ADQVIIATGG IGQLYSATSN CLEATGDGIA MAYRAGAAIC DMEFIQFHPT LLMNGDSSCG
     LISEAVRGEG GRLVTEDGQF LMKGKHSLED LAPRDVVARE IFNTKLNNNK IFLNINNVAN
     FQYRFPSIYE MCKKTPELLK SGLLPVQPGA HFIMGGVKVD RDGRSSIENL FAVGECAYTG
     VHGANRLASN SLLEAIVFAE RLASTILGAE KIKRDGGRVP VVMKTFNNLP LPTKTEIQEV
     MDRYVGIMRD KEGLQKAVSW FDQFKDISME QSHFQLSVED KIICNMLISG SLIARASLMR
     EESRGGHYRS DYPTTNDKKW YGYQNVFLNG DLYCEKFFEL SEMIG
//

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