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Database: UniProt
Entry: A0A069JTF2_9ACTN
LinkDB: A0A069JTF2_9ACTN
Original site: A0A069JTF2_9ACTN 
ID   A0A069JTF2_9ACTN        Unreviewed;       594 AA.
AC   A0A069JTF2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=DT87_12465 {ECO:0000313|EMBL:KDQ67988.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ67988.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ67988.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ67988.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-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:KDQ67988.1}.
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DR   EMBL; JJOB01000001; KDQ67988.1; -; Genomic_DNA.
DR   RefSeq; WP_037877808.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069JTF2; -.
DR   OrthoDB; 9805351at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000027475; 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   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   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}.
FT   DOMAIN          18..397
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          446..553
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          416..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   594 AA;  61233 MW;  AB701F334F3DA7D3 CRC64;
     MTGIRLTAPA PGWSIDADVV VVGSGVAGLT TALRCAAAGL ATVVVTKARL DDGSTRWAQG
     GIAAALGEGD TPEQHLDDTL VAGAGLCDEA AVRALVTEGP GAMSRLIGTG ARFDTTEAGA
     LALTREGGHH RRRIAHAGGD ATGAEVSRAL VGAVRSAALR TIENALVLDL LTDAEGRTTG
     VTLHVMGEGQ HDGVGAVRAP AVVLATGGMG QVFSATTNPP VSTGDGVALA LRAGAEVSDL
     EFVQFHPTVL FLGAGAEGQQ PLVSEAVRGE GAHLVDASGT RFMLGQHELA ELAPRDIVAK
     AITRQMRLTG TEHMYLDARH FGAEMWARRF PTILAACRAH GIDPVTEPVP VAPAAHYASG
     GVRTDLWGRT TVPGLYACGE TACTGVHGAN RLASNSLLEG LVFAERIAAD IVAAGPQERG
     AEPAPERADG QGPAPASVPL LAAESRTAVQ RIMTRGAGVI RSASSLAEAA ERLEALGRTA
     SASGTDAEDA AKDAVPGVEA WEATNLLLVS QVLVAAARER EETRGCHWRE DRPDRDDTAW
     RRHLVVRTGP DGRPVVSRTR DAAFPPVRPG APADPAGPTD LPNHPAEAPQ EPQP
//
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