ID LGOX_STRSQ Reviewed; 701 AA. AC Q8L3C7; DT 03-MAY-2023, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 02-OCT-2024, entry version 71. DE RecName: Full=L-glutamate oxidase precursor {ECO:0000303|Ref.2}; DE Short=LGOX {ECO:0000303|PubMed:14769868}; DE EC=1.4.3.11 {ECO:0000269|PubMed:14769868, ECO:0000269|PubMed:22197816, ECO:0000269|Ref.2}; DE Contains: DE RecName: Full=L-glutamate oxidase alpha chain {ECO:0000305|PubMed:19531050}; DE Contains: DE RecName: Full=L-glutamate oxidase gamma chain {ECO:0000305|PubMed:19531050}; DE Contains: DE RecName: Full=L-glutamate oxidase beta chain {ECO:0000305|PubMed:19531050}; DE Flags: Precursor; GN Name=lgoX {ECO:0000303|PubMed:14769868}; OS Streptomyces sp. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1931; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-33; 395-407 AND RP 523-533, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PROTEOLYTIC CLEAVAGE. RC STRAIN=X-119-6; 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] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PROTEOLYTIC CLEAVAGE. RC STRAIN=X-119-6; RX DOI=10.1080/00021369.1983.10866079; RA Kusakabe H., Midorikawa Y., Fujishima T., Kuninaka A., Yoshino H.; RT "Purification and properties of a new enzyme, L-glutamate oxidase, from RT Streptomyces sp. X-119-6 grown on wheat bran."; RL Agric. Biol. Chem. 47:1323-1328(1983). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ARG-305; HIS-312 AND TRP-564. RC STRAIN=X-119-6; RX PubMed=22197816; DOI=10.1016/j.bbrc.2011.12.033; RA Utsumi T., Arima J., Sakaguchi C., Tamura T., Sasaki C., Kusakabe H., RA Sugio S., Inagaki K.; RT "Arg305 of Streptomyces L-glutamate oxidase plays a crucial role for RT substrate recognition."; RL Biochem. Biophys. Res. Commun. 417:951-955(2012). RN [4] {ECO:0007744|PDB:2E1M} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 15-390; 391-520 AND 521-701 IN RP COMPLEX WITH FAD, COFACTOR, SUBUNIT, DOMAIN, AND PROTEOLYTIC CLEAVAGE. RC STRAIN=X-119-6; 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 [5] {ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 16-701 OF MUTANT GLU-305 IN RP COMPLEXES WITH FAD AND L-ARGININE, BIOTECHNOLOGY, AND MUTAGENESIS OF RP ARG-305. 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 -!- FUNCTION: Catalyzes the oxidative deamination of L-glutamate to 2- CC ketoglutarate along with the production of ammonia and hydrogen CC peroxide (PubMed:14769868, PubMed:22197816, Ref.2). Shows strict CC substrate specificity for L-glutamate, and exhibits only very weak CC activity with L-aspartate (Ref.2). {ECO:0000269|PubMed:14769868, CC ECO:0000269|PubMed:22197816, ECO:0000269|Ref.2}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985; EC=1.4.3.11; CC Evidence={ECO:0000269|PubMed:14769868, ECO:0000269|PubMed:22197816, CC ECO:0000269|Ref.2}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:19531050, ECO:0000269|Ref.2}; CC -!- ACTIVITY REGULATION: Produced as a single polypeptide precursor and is CC activated by proteolytic cleavage (PubMed:14769868). The LGOX precursor CC is an active enzyme, but it exhibits lower catalytic efficiency and CC lower thermostability compared with the mature hexameric LGOX CC (PubMed:14769868). The mature form is strongly inhibited by p- CC chloromercuribenzoate, but not by CuCl(2), EDTA and CC diethyldithiocarbamate (Ref.2). {ECO:0000269|PubMed:14769868, CC ECO:0000269|Ref.2}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.21 mM for L-glutamate (mature LGOX) {ECO:0000269|Ref.2}; CC KM=0.173 mM for L-glutamate (mature LGOX) CC {ECO:0000269|PubMed:22197816}; CC KM=0.23 mM for L-glutamate (at pH 6.0 for recombinant LGOX expressed CC in E.coli) {ECO:0000269|PubMed:14769868}; CC KM=5 mM for L-glutamate (at pH 7.4 for recombinant LGOX expressed in CC E.coli) {ECO:0000269|PubMed:14769868}; CC KM=29 mM for L-aspartate (mature LGOX) {ECO:0000269|Ref.2}; CC Note=kcat is 53.2 sec(-1) for mature LGOX. CC {ECO:0000269|PubMed:22197816}; CC pH dependence: CC Optimum pH is 7.0-8.0 for mature LGOX (Ref.2). Optimum pH is 7.0 for CC recombinant LGOX expressed in E.coli (PubMed:14769868). CC {ECO:0000269|PubMed:14769868, ECO:0000269|Ref.2}; CC Temperature dependence: CC Optimum temperature is 35 degrees Celsius at pH 7.4 and 50 degrees CC Celsius at pH 6.0 for recombinant LGOX expressed in E.coli. CC {ECO:0000269|PubMed:14769868}; CC -!- SUBUNIT: The LGOX precursor forms homodimers (PubMed:14769868). The CC mature enzyme is a heterohexamer composed of 2 alpha chains, 2 beta CC chains and 2 gamma chains (alpha2beta2gamma2) (PubMed:14769868, CC PubMed:19531050, Ref.2). {ECO:0000269|PubMed:14769868, CC ECO:0000269|PubMed:19531050, ECO:0000269|Ref.2}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:14769868}. CC -!- DOMAIN: Contains a deeply buried active site and two entrances from the CC surface of the protein into the active site. CC {ECO:0000269|PubMed:19531050}. CC -!- PTM: The precursor form is proteolytically cleaved by an endopeptidase CC into alpha, beta and gamma chains, which form the stable mature enzyme CC (PubMed:14769868, PubMed:19531050, Ref.2). Activation by proteolysis CC occurs after secretion (Probable). {ECO:0000269|PubMed:14769868, CC ECO:0000269|PubMed:19531050, ECO:0000269|Ref.2, CC ECO:0000305|PubMed:14769868}. CC -!- BIOTECHNOLOGY: LGOX has been used as a biosensor to quantify L- CC glutamate and been applied in quality management of foods and CC fermentation processes, and can also be used in biosensors for clinical CC testing apparatus. The alternation of substrate specificity expands the CC application range of LGOX in industrial, medical and pharmaceutical CC fields. The LGOX R305E mutant is suitable for the determination of L- CC arginine. {ECO:0000269|PubMed:33764624}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. LGOX CC subfamily. {ECO:0000305}. 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 PDBsum; 7E0C; -. DR PDBsum; 7E0D; -. DR AlphaFoldDB; Q8L3C7; -. DR SMR; Q8L3C7; -. DR MINT; Q8L3C7; -. DR BRENDA; 1.4.3.11; 1284. DR EvolutionaryTrace; Q8L3C7; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:TreeGrafter. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009063; P:amino acid catabolic process; IEA:TreeGrafter. DR Gene3D; 1.10.10.1620; -; 1. DR Gene3D; 1.10.10.1790; -; 1. DR Gene3D; 3.30.1490.470; -; 1. DR Gene3D; 3.30.160.490; -; 1. DR Gene3D; 3.30.70.2100; -; 1. DR Gene3D; 6.10.140.1210; -; 1. DR Gene3D; 6.10.250.1500; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR050281; Flavin_monoamine_oxidase. DR PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR Pfam; PF01593; Amino_oxidase; 2. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; KW Nucleotide-binding; Oxidoreductase; Secreted; Signal; Zymogen. FT SIGNAL 1..14 FT /evidence="ECO:0000305|PubMed:19531050" FT CHAIN 15..701 FT /note="L-glutamate oxidase precursor" FT /id="PRO_0000457963" FT CHAIN 15..390 FT /note="L-glutamate oxidase alpha chain" FT /evidence="ECO:0000305|PubMed:19531050" FT /id="PRO_0000457964" FT CHAIN 391..480 FT /note="L-glutamate oxidase gamma chain" FT /evidence="ECO:0000305|PubMed:19531050" FT /id="PRO_0000457965" FT PROPEP 481..520 FT /evidence="ECO:0000305|PubMed:19531050" FT /id="PRO_0000457966" FT CHAIN 521..683 FT /note="L-glutamate oxidase beta chain" FT /evidence="ECO:0000305|PubMed:19531050" FT /id="PRO_0000457967" FT PROPEP 684..701 FT /evidence="ECO:0000305|PubMed:19531050" FT /id="PRO_0000457968" FT BINDING 69 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 88 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:33764624, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 97 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 123 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 124 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 354 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 409 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 645 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 653 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT BINDING 654 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:19531050, FT ECO:0000269|PubMed:33764624, ECO:0007744|PDB:2E1M, FT ECO:0007744|PDB:7E0C, ECO:0007744|PDB:7E0D" FT SITE 305 FT /note="Important for substrate specificity" FT /evidence="ECO:0000269|PubMed:22197816, FT ECO:0000269|PubMed:33764624" FT MUTAGEN 305 FT /note="R->A: 20-fold decrease in L-glutamate oxidation. FT Changes substrate specificity, the mutant can use L- FT histidine, L-phenylalanine and L-leucine." FT /evidence="ECO:0000269|PubMed:22197816" FT MUTAGEN 305 FT /note="R->D: Strong decrease in L-glutamate oxidation. FT Changes substrate specificity, the mutant can use L- FT arginine, L-histidine, L-phenylalanine and L-leucine." FT /evidence="ECO:0000269|PubMed:22197816" FT MUTAGEN 305 FT /note="R->E: Exhibits strict specificity for L-arginine." FT /evidence="ECO:0000269|PubMed:33764624" FT MUTAGEN 305 FT /note="R->K: Strong decrease in L-glutamate oxidation. FT Changes substrate specificity, the mutant can use L- FT histidine, L-phenylalanine and L-leucine." FT /evidence="ECO:0000269|PubMed:22197816" FT MUTAGEN 305 FT /note="R->L: Strong decrease in L-glutamate oxidation. FT Changes substrate specificity, the mutant can use L- FT histidine, L-phenylalanine, L-leucine and L-asparagine." FT /evidence="ECO:0000269|PubMed:22197816" FT MUTAGEN 312 FT /note="H->A: Strong decrease in L-glutamate oxidation. Has FT little influence on substrate specificity." FT /evidence="ECO:0000269|PubMed:22197816" FT MUTAGEN 564 FT /note="W->A: Strong decrease in L-glutamate oxidation. Has FT little influence on substrate specificity." FT /evidence="ECO:0000269|PubMed:22197816" FT HELIX 18..28 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 39..48 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:7E0D" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 205..210 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 223..227 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 230..242 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 259..273 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 278..284 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 290..299 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 310..315 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 335..342 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 343..347 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 348..359 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 394..403 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 407..410 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 421..429 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 435..444 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 451..459 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 465..469 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 541..544 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 556..564 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 565..572 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 576..591 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 593..598 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 599..607 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 608..610 FT /evidence="ECO:0007829|PDB:7E0C" FT TURN 612..614 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 625..634 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 640..642 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:7E0C" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:7E0C" FT HELIX 654..670 FT /evidence="ECO:0007829|PDB:7E0C" 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 //