ID A0A0D9YLY8_9ORYZ Unreviewed; 761 AA.
AC A0A0D9YLY8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G02710.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G02710.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G02710.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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|RuleBase:RU362049};
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: Plastid, chloroplast
CC {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 AlphaFoldDB; A0A0D9YLY8; -.
DR STRING; 40148.A0A0D9YLY8; -.
DR EnsemblPlants; OGLUM02G02710.1; OGLUM02G02710.1; OGLUM02G02710.
DR Gramene; OGLUM02G02710.1; OGLUM02G02710.1; OGLUM02G02710.
DR eggNOG; KOG2403; Eukaryota.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; 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:UP000026961}.
FT DOMAIN 202..586
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 642..728
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 761 AA; 83663 MW; 9AE77568F2EE21ED CRC64;
MWRLGVRGIF LAFPFLSKAK STFWLLFFTH PSSSSLLSPN QSPSRILLLL RKPSPDVVSD
TQRLCLISAR HLSSSSCCAR ACFFFPLSQR AVLGAGEAPR SPSSSSCDSA KSLEPGMAAL
MNGFGSLQCK AMVHVEKGHM QASGMAFFSP VNRCAQVHIS SIPRFIGAKS VSASQLRMRH
KVGSIRASAA SCLQDDTTKY FDFVVIGSGV AGLRYALEVS KYGSVAIITK AEPHESNTNY
AQGGVSAVLC PSDSVESHMQ DTIVAGAYLC DEETVRVVCT EGPERVKELI AMGASFDHGE
DGRLHLAREG GHSHNRIVHS ADMTGREIER ALLQAVDNDD NISLFGHHFA IDLLTCQSNG
EIYCYGVDSL DAETQKAIRF ISKVTLLASG GVGHIYPSTT NPPVATGDGI AMSHRAQAVI
SNMEFVQFHP TALSDEGLPI KPATRRENAF LITEAVRGDG GILYNQSMER FMTSYDDRAE
LAPRDVVARS IDDQLKKRGE KYVLLDISHK PREKVLAHFP NIAAECLRHG LDITQQPIPV
VPAAHYMCGG VRAGLQGETN VKGLYVAGEV ACTGLHGANR LASNSLLEAL VFARRAVQPS
IDHMVDADVD PSFAKKWARP VLSVSLRDSI LSDIIEKTKQ ARMELQSIMW EYVGIVRSTN
RLKHAEWKIS DLESEWVEFL FRRGWKPTMV GVETCEMRNL FCCAKLVVKS ALARHESRGL
HFTEDFPYLE ESKRKPTVIF PAHIQELTWS SKPLQKQLQC K
//
