GenomeNet

Database: UniProt
Entry: OXLA_NAJAT
LinkDB: OXLA_NAJAT
Original site: 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-MAY-2023, entry version 51.
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}.
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; 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: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   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
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; 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
//
DBGET integrated database retrieval system