ID Q8L3C7_9ACTN Unreviewed; 701 AA. AC Q8L3C7; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 14-DEC-2022, entry version 64. DE SubName: Full=L-glutamate oxidase {ECO:0000313|EMBL:BAB93449.1}; GN Name=Lgox {ECO:0000313|EMBL:BAB93449.1}; OS Streptomyces sp. X-119-6. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=196112 {ECO:0000313|EMBL:BAB93449.1}; RN [1] {ECO:0000313|EMBL:BAB93449.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=X-119-6 {ECO:0000313|EMBL:BAB93449.1}; RX PubMed=14769868; DOI=10.1093/jb/mvg206; RA Arima J., Tamura T., Kusakabe H., Ashiuchi M., Yagi T., Tanaka H., RA Inagaki K.; RT "Recombinant expression, biochemical characterization and stabilization RT through proteolysis of an L-glutamate oxidase from Streptomyces sp. X-119- RT 6."; RL J. Biochem. 134:805-812(2003). RN [2] {ECO:0007829|PDB:2E1M} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 15-390; 391-520 AND 521-701 IN RP COMPLEX WITH FAD. RX PubMed=19531050; DOI=10.1111/j.1742-4658.2009.07103.x; RA Arima J., Sasaki C., Sakaguchi C., Mizuno H., Tamura T., Kashima A., RA Kusakabe H., Sugio S., Inagaki K.; RT "Structural characterization of L-glutamate oxidase from Streptomyces sp. RT X-119-6."; RL FEBS J. 276:3894-3903(2009). RN [3] {ECO:0007829|PDB:7E0C, ECO:0007829|PDB:7E0D} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 16-701. RX PubMed=33764624; DOI=10.1002/pro.4070; RA Yano Y., Matsuo S., Ito N., Tamura T., Kusakabe H., Inagaki K., Imada K.; RT "A new l-arginine oxidase engineered from l-glutamate oxidase."; RL Protein Sci. 30:1044-1055(2021). 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; AB085623; BAB93449.1; -; Genomic_DNA. DR PDB; 2E1M; X-ray; 2.80 A; A=15-390, B=391-520, C=521-701. DR PDB; 7E0C; X-ray; 2.65 A; A=16-701. DR PDB; 7E0D; X-ray; 2.70 A; A=16-701. DR PDBsum; 2E1M; -. DR AlphaFoldDB; Q8L3C7; -. DR SMR; Q8L3C7; -. DR MINT; Q8L3C7; -. DR BRENDA; 1.4.3.11; 1284. DR EvolutionaryTrace; Q8L3C7; -. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR Pfam; PF01593; Amino_oxidase; 2. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2E1M, ECO:0007829|PDB:7E0C}; KW FAD {ECO:0007829|PDB:2E1M}; Flavoprotein {ECO:0007829|PDB:2E1M}; KW Nucleotide-binding {ECO:0007829|PDB:2E1M}. FT DOMAIN 68..448 FT /note="Amino_oxidase" FT /evidence="ECO:0000259|Pfam:PF01593" FT DOMAIN 531..668 FT /note="Amino_oxidase" FT /evidence="ECO:0000259|Pfam:PF01593" FT BINDING 69 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 88 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 97 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 121 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 123 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 124 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 354 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 409 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 608 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 645 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 653 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" FT BINDING 654 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:2E1M" SQ SEQUENCE 701 AA; 77891 MW; A7C930462AA3609A CRC64; MTTDTARRHT GAERANEMTY EQLARELLLV GPAPTNEDLK LRYLDVLIDN GLNPPGPPKR ILIVGAGIAG LVAGDLLTRA GHDVTILEAN ANRVGGRIKT FHAKKGEPSP FADPAQYAEA GAMRLPSFHP LTLALIDKLG LKRRLFFNVD IDPQTGNQDA PVPPVFYKSF KDGKTWTNGA PSPEFKEPDK RNHTWIRTNR EQVRRAQYAT DPSSINEGFH LTGCETRLTV SDMVNQALEP VRDYYSVKQD DGTRVNKPFK EWLAGWADVV RDFDGYSMGR FLREYAEFSD EAVEAIGTIE NMTSRLHLAF FHSFLGRSDI DPRATYWEIE GGSRMLPETL AKDLRDQIVM GQRMVRLEYY DPGRDGHHGE LTGPGGPAVA IQTVPEGEPY AATQTWTGDL AIVTIPFSSL RFVKVTPPFS YKKRRAVIET HYDQATKVLL EFSRRWWEFT EADWKRELDA IAPGLYDYYQ QWGEDDAEAA LALPQSVRNL PTGLLGAHPS VDESRIGEEQ VEYYRNSELR GGVRPATNAY GGGSTTDNPN RFMYYPSHPV PGTQGGVVLA AYSWSDDAAR WDSFDDAERY GYALENLQSV HGRRIEVFYT GAGQTQSWLR DPYACGEAAV YTPHQMTAFH LDVVRPEGPV YFAGEHVSLK HAWIEGAVET AVRAAIAVNE APVGDTGVTA AAGRRGAAAA TEPMREEALT S //