GenomeNet

Database: UniProt
Entry: A0A1J1LER3_9CYAN
LinkDB: A0A1J1LER3_9CYAN
Original site: A0A1J1LER3_9CYAN 
ID   A0A1J1LER3_9CYAN        Unreviewed;       570 AA.
AC   A0A1J1LER3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:CUR31053.1};
GN   ORFNames=PL9214290644 {ECO:0000313|EMBL:CUR31053.1};
OS   Planktothrix tepida PCC 9214.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR31053.1, ECO:0000313|Proteomes:UP000184315};
RN   [1] {ECO:0000313|Proteomes:UP000184315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Regsiter A., william w.;
RL   Submitted (OCT-2015) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CZDF01000132; CUR31053.1; -; Genomic_DNA.
DR   RefSeq; WP_072717983.1; NZ_LN889782.1.
DR   AlphaFoldDB; A0A1J1LER3; -.
DR   STRING; 671072.PL9214290644; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000184315; 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   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:UP000184315}.
FT   DOMAIN          17..393
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          446..559
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   570 AA;  62891 MW;  7DAA41198EBB2B91 CRC64;
     MTVIETSLTS HLPLVFDVLV VGTGAAGLYT ALCLPEHLKI GLVSKDALPL SASDWAQGGI
     AAAISSDDSP TLHLEDTLKA GAGLCEVEAV QFLVNHAPKC IHRLVELGVA FDRHQSQLAL
     TLEAAHSRHR VLHAADTTGR AVITTLTERV LERPNIKIIS PAFALDLWMD TDGQRCQGIS
     LIHNHQIYRV KAKAVILATG GGGQVFAHTT NPEVSTGDGV AIAWRAGALL RDLEFFQFHP
     TALTQPGAPR FLISEAVRGE GAHLIDSQGR RFVFDYDSRG ELAPRDVVSR AIFNHLQQLR
     QQPGNHGEQV WLDLRSIPPD KIRYRFPNII QVCQQWGIDI LNQPIPVTPA AHYWMGGIVT
     DTQGQTSIPG LYAVGETAST GVHGANRLAS NSLLECLVFG AQLASIDFRN LPTTKEKFDS
     TLEIKPVILS DSHWEEHYAR IKTIRSHLPH VLWQSAGICR QSDHLEEGLT QVKAWSEEFL
     ALPISQLLSR VHPSDSSHWE LVGIKAHDLK QWGETRNLLS IGELILKSAA FRLESRGGHY
     RQDYPQSDPS WQVHTLIQEN QIWKSPPVPD
//
DBGET integrated database retrieval system