ID OXLA_GLOHA Reviewed; 504 AA. AC Q6STF1; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 03-MAY-2023, entry version 86. DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:15103157}; DE Short=AHP-LAAO {ECO:0000303|PubMed:15103157}; DE Short=LAO; DE EC=1.4.3.2 {ECO:0000269|PubMed:15103157}; DE Flags: Precursor; OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius. OX NCBI_TaxID=8714; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RA Zhang H., Zhang T., Teng M., Niu L.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000312|PDB:1REO} RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 19-504 IN COMPLEX WITH FAD, RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND RP ASN-379, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR RP LOCATION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Venom; RX PubMed=15103157; DOI=10.1107/s0907444904000046; RA Zhang H., Teng M., Niu L., Wang Y., Wang Y., Liu Q., Huang Q., Hao Q., RA Dong Y., Liu P.; RT "Purification, partial characterization, crystallization and structural RT determination of AHP-LAAO, a novel L-amino-acid oxidase with cell RT apoptosis-inducing activity from Agkistrodon halys pallas venom."; RL Acta Crystallogr. D 60:974-977(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-504 IN COMPLEX WITH FAD AND RP SUBSTRATE ANALOGS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-190 AND RP ASN-379. RA Zhang H., Teng M., Niu L.; RT "Structures of L-amino acid oxidase in complex with substrates and RT substrate analogue."; RL Submitted (MAY-2004) to the PDB data bank. CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly CC hydrophobic and aromatic L-amino acids, thus producing hydrogen CC peroxide that may contribute to the diverse toxic effects of this CC enzyme (PubMed:15103157). Shows activity on L-Leu (PubMed:15103157). CC Exhibits diverse biological activities, such as hemorrhage, hemolysis, CC edema, antibacterial and antiparasitic activities, as well as CC regulation of platelet aggregation (By similarity). Its effect on CC platelets is controversial, since it either induces aggregation or CC inhibits agonist-induced aggregation (By similarity). These different CC effects are probably due to different experimental conditions (By CC similarity). This protein induces apoptosis of cultured HeLa cells CC (PubMed:15103157). {ECO:0000250|UniProtKB:P0CC17, CC ECO:0000269|PubMed:15103157}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, CC ChEBI:CHEBI:59869; EC=1.4.3.2; CC Evidence={ECO:0000269|PubMed:15103157}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:15103157}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:15103157}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.25 mM for L-Leu {ECO:0000269|PubMed:15103157}; CC pH dependence: CC Optimum pH is 8.8. {ECO:0000269|PubMed:15103157}; CC -!- SUBUNIT: Homodimer; non-covalently linked. CC {ECO:0000250|UniProtKB:P81382}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15103157}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:15103157}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 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; AY450403; AAR20248.1; -; mRNA. DR PDB; 1REO; X-ray; 2.31 A; A=19-504. DR PDB; 1TDK; X-ray; 2.70 A; A=19-504. DR PDB; 1TDN; X-ray; 2.70 A; A=19-504. DR PDB; 1TDO; X-ray; 3.00 A; A=19-504. DR PDBsum; 1REO; -. DR PDBsum; 1TDK; -. DR PDBsum; 1TDN; -. DR PDBsum; 1TDO; -. DR AlphaFoldDB; Q6STF1; -. DR SMR; Q6STF1; -. DR iPTMnet; Q6STF1; -. DR EvolutionaryTrace; Q6STF1; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR Gene3D; 3.90.660.10; -; 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 PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR Pfam; PF01593; Amino_oxidase; 1. 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; Antibiotic; Antimicrobial; Apoptosis; Cytolysis; KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein; KW Hemolysis; Hemorrhagic toxin; Hemostasis impairing toxin; Oxidoreductase; KW Secreted; Signal; Toxin. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:15103157" FT CHAIN 19..504 FT /note="L-amino-acid oxidase" FT /id="PRO_0000273563" FT BINDING 61..62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 81..82 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 105..108 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1TDK, FT ECO:0007744|PDB:1TDN, ECO:0007744|PDB:1TDO" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1TDK" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 390 FT /ligand="substrate" FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:1TDN" FT BINDING 475 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 482..487 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT BINDING 482..483 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT DISULFID 28..191 FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT DISULFID 349..430 FT /evidence="ECO:0000269|PubMed:15103157, ECO:0000269|Ref.3" FT HELIX 26..29 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 34..43 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 61..72 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:1REO" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:1TDN" FT HELIX 114..122 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 148..153 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 171..178 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 180..188 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 191..197 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 203..209 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:1TDO" FT HELIX 235..245 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 278..285 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 300..310 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 314..318 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 328..336 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 342..351 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 353..357 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 385..392 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 393..397 FT /evidence="ECO:0007829|PDB:1REO" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 404..419 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 423..429 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 430..437 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:1REO" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 455..464 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:1REO" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:1REO" FT HELIX 484..503 FT /evidence="ECO:0007829|PDB:1REO" SQ SEQUENCE 504 AA; 57125 MW; AEB034155184F0A7 CRC64; MNVFFMFSLL FLAALGSCAN DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVVVGAG MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEDW YANLGPMRLP EKHRIVREYI RKFGLQLNEF SQENDNAWYF IKNIRKRVGE VKKDPGVLKY PVKPSEEGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR HDDIFAYEKR FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS ESLTASVDRI YFAGEHTAEA HGWIDSTIKS GLRAARDVNR ASEQ //