ID Q8L3C7_9ACTN Unreviewed; 701 AA. AC Q8L3C7; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 05-JUL-2017, entry version 51. 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 RT stabilization through proteolysis of an L-glutamate oxidase from RT Streptomyces sp. X-119-6."; RL J. Biochem. 134:805-812(2003). RN [2] {ECO:0000213|PDB:2E1M} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 15-390; 391-520 AND 521-701 RP IN 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 RT sp. X-119-6."; RL FEBS J. 276:3894-3903(2009). 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 ProteinModelPortal; Q8L3C7; -. DR SMR; Q8L3C7; -. DR MINT; MINT-7041554; -. 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 InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01593; Amino_oxidase; 2. DR SUPFAM; SSF51905; SSF51905; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2E1M}; FAD {ECO:0000213|PDB:2E1M}; KW Flavoprotein {ECO:0000213|PDB:2E1M}; KW Nucleotide-binding {ECO:0000213|PDB:2E1M}. FT DOMAIN 68 448 Amino_oxidase. {ECO:0000259|Pfam: FT PF01593}. FT DOMAIN 531 668 Amino_oxidase. {ECO:0000259|Pfam: FT PF01593}. FT NP_BIND 88 89 FAD. {ECO:0000213|PDB:2E1M}. FT NP_BIND 121 124 FAD. {ECO:0000213|PDB:2E1M}. FT NP_BIND 653 654 FAD. {ECO:0000213|PDB:2E1M}. FT BINDING 69 69 FAD; via amide nitrogen. FT {ECO:0000213|PDB:2E1M}. FT BINDING 97 97 FAD. {ECO:0000213|PDB:2E1M}. FT BINDING 354 354 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000213|PDB:2E1M}. FT BINDING 409 409 FAD. {ECO:0000213|PDB:2E1M}. FT BINDING 608 608 FAD. {ECO:0000213|PDB:2E1M}. FT BINDING 645 645 FAD; via amide nitrogen. FT {ECO:0000213|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 //