OXLA_NAJAT
ID OXLA_NAJAT Reviewed; 507 AA.
AC A8QL58; A0A2R4N4Q6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:17543361};
DE Short=LAO;
DE Short=NA-LAAO {ECO:0000303|PubMed:18180850};
DE EC=1.4.3.2 {ECO:0000269|PubMed:18180850};
DE Flags: Precursor; Fragment;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1] {ECO:0000312|EMBL:AVX27607.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Chiang L.C., Mao Y.C.-C., Wu W.G.;
RT "Isolation and characterization of L-amino acid oxidase from Naja atra
RT snake venom.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABN72546.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-449.
RC TISSUE=Venom gland;
RX PubMed=17543361; DOI=10.1016/j.toxicon.2007.04.013;
RA Jin Y., Lee W.-H., Zeng L., Zhang Y.;
RT "Molecular characterization of L-amino acid oxidase from king cobra
RT venom.";
RL Toxicon 50:479-489(2007).
RN [3]
RP PROTEIN SEQUENCE OF 20-29, FUNCTION IN PLATELET AGGREGATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Venom;
RX PubMed=18180850; DOI=10.1111/j.1745-7270.2008.00372.x;
RA Li R., Zhu S., Wu J., Wang W., Lu Q., Clemetson K.J.;
RT "L-amino acid oxidase from Naja atra venom activates and binds to human
RT platelets.";
RL Acta Biochim. Biophys. Sin. 40:19-26(2008).
RN [4] {ECO:0007744|PDB:5Z2G}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH FAD, GLYCOSYLATION
RP AT ASN-191; ASN-213 AND ASN-378, DISULFIDE BONDS, COFACTOR, AND SUBUNIT.
RA Kumar J.V., Chien K.Y., Lin C.C., Chiang L.C., Lin T.H., Wu W.G.;
RT "Crystal structure of L-amino acid oxidase from naja atra (Taiwan Cobra).";
RL Submitted (JAN-2018) 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:18180850). Shows activity on L-Leu (PubMed:18180850).
CC Exhibits diverse biological activities, such as hemorrhage, hemolysis,
CC edema, apoptosis of vascular endothelial cells or tumor cell lines,
CC antibacterial and antiparasitic activities (By similarity). This
CC protein induces platelet aggregation by both hydrogen peroxide
CC production and binding to platelet membrane proteins (that would
CC enhance the sensitivity of platelets to hydrogen peroxide). Effects of
CC snake L-amino oxidases on platelets are controversial, since they
CC either induce aggregation or inhibit agonist-induced aggregation. These
CC different effects are probably due to different experimental
CC conditions. {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:18180850}.
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:18180850};
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:18180850};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=38.4 umol/min/mg enzyme {ECO:0000269|PubMed:18180850};
CC -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18180850}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18180850}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; EF080839; ABN72546.1; -; mRNA.
DR EMBL; MH023324; AVX27607.1; -; mRNA.
DR PDB; 5Z2G; X-ray; 2.68 A; A/B=1-507.
DR PDBsum; 5Z2G; -.
DR AlphaFoldDB; A8QL58; -.
DR SMR; A8QL58; -.
DR BRENDA; 1.4.3.2; 3558.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 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; Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:18180850"
FT CHAIN 20..>507
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412603"
FT BINDING 62..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382,
FT ECO:0007744|PDB:5Z2G"
FT BINDING 82..83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382,
FT ECO:0007744|PDB:5Z2G"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT BINDING 106..109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382,
FT ECO:0007744|PDB:5Z2G"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT BINDING 480..485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382,
FT ECO:0007744|PDB:5Z2G"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:5Z2G"
FT DISULFID 29..192
FT /evidence="ECO:0007744|PDB:5Z2G"
FT DISULFID 348..429
FT /evidence="ECO:0007744|PDB:5Z2G"
FT CONFLICT 28..38
FT /note="KCFQEADYEDF -> ECFQQNDYEEI (in Ref. 2; ABN72546)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="E -> K (in Ref. 2; ABN72546)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="S -> P (in Ref. 2; ABN72546)"
FT /evidence="ECO:0000305"
FT NON_TER 507
FT /evidence="ECO:0000303|Ref.1"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5Z2G"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 290..309
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 341..350
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:5Z2G"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:5Z2G"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:5Z2G"
FT HELIX 482..499
FT /evidence="ECO:0007829|PDB:5Z2G"
SQ SEQUENCE 507 AA; 57963 MW; 4A67EDCDF9502A22 CRC64;
MNVLFIFSLL FLAALESCAD DRRSPLEKCF QEADYEDFLE IARNGLKETS NPKHVVVVGA
GMAGLSAAYV LAGAGHKVTL LEASERVGGR VITYHNDREG WYVNMGPMRL PERHRIVREY
IRKFGLKLNE FFQENENAWY YINNIRKRVW EVKKDPSLLK YPVKPSEEGK SASQLYQESL
RKVIEELKRT NCSYILNKYD SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYHLSFMESL
KSDALFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNARV IKIQYDAEKV RVTYQTPAKT
FVTADYVIVC STSRAARRIY FEPPLPPKKA HALRSIHYRS ATKIFLTCSK KFWEADGIHG
GKSTTDLPSR FIHYPNHNFT SGIGVIMAYV LADDSDFFQA LDTKTCADIV INDLSLIHDL
PKREIQALCY PSIKKWNLDK YTMGSITSFT PYQFQDYFES AAAPVGRIHF AGEYTGRFHG
WIDSTIMTGL RAARDVNRAS QKPSKIR
