OXLA_GLOHA
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-AUG-2022, entry version 82.
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}.
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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 PRIDE; 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: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 Pfam; PF01593; Amino_oxidase; 1.
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; 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
