ID   OXLA_PSEAU              Reviewed;         517 AA.
AC   Q4JHE1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   Flags: Precursor;
OS   Pseudechis australis (Mulga snake) (King brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=8670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA   St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT   "Identification and analysis of venom gland-specific genes from the
RT   coastal taipan (Oxyuranus scutellatus) and related species.";
RL   Cell. Mol. Life Sci. 62:2679-2693(2005).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=1796476; DOI=10.1016/0041-0101(91)90210-I;
RA   Stiles B.G., Sexton F.W., Weinstein S.A.;
RT   "Antibacterial effects of different snake venoms: purification and
RT   characterization of antibacterial proteins from Pseudechis australis
RT   (Australian king brown or mulga snake) venom.";
RL   Toxicon 29:1129-1141(1991).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Inhibits platelet
CC       aggregation. Has an ability to induce apoptosis and hemorrhage (By
CC       similarity). Has an antibacterial activity.
CC   -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid
CC       + NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   EMBL; DQ088992; AAY89682.1; -; mRNA.
DR   SMR; Q4JHE1; 23-504.
DR   HOVERGEN; Q4JHE1; -.
DR   BRENDA; 1.4.3.2; 276288.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR001613; Amineoxid_fl.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW   Secreted; Signal; Toxin.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    517       L-amino-acid oxidase.
FT                                /FTId=PRO_5000140380.
FT   NP_BIND     108    109       FAD (By similarity).
FT   NP_BIND     485    488       FAD (By similarity).
FT   BINDING      82     82       FAD (By similarity).
FT   BINDING      90     90       FAD (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     280    280       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     391    391       Substrate (By similarity).
FT   BINDING     476    476       FAD (By similarity).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   DISULFID     29    192       By similarity.
FT   DISULFID    350    431       By similarity.
SQ   SEQUENCE   517 AA;  58744 MW;  9E0ACCD728782BE5 CRC64;
     MNVFFMFSLL FLAALGSCAD DRRRPLEECF READYEEFLE IAKNGLQRTS NPKRVVVVGA
     GMAGLSAAYV LAGAGHQVTL LEASERVGGR VNTYRNEKDG WYVNLGPMRL PERHRIIREY
     IRKFGLELNE FIQENDNAWY FIKNIRKRVS EVKKDPGVFK YPVKPSEEGK SASQLYRESL
     QKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSPGAVD MIGDLLNEDS SYYLSFIESL
     KSDDIFSYEK RFDEIVGGFD QLPRSMYQAI AEKVHLNAQV IKIQQNAEDV RVTYQTPAKT
     LSYVIADYVI VCSTSRAARR IHFEPPLPPK KAHALRSIHY RSSTKIFLTC SQKFWEADGI
     HGGKSTTDLP SRFIYYPNHS FTSGIGVIVA YTLADDTDFF QALDIETSAD IVINDLSLIH
     QLPKEQIQAL CYPSKIQKWS LDEYAMGAIT SFTPYQFQDF FEIVAAPVGR IYFAGEYTAS
     VHGWLDSTIK SGLTAARDVN LASQKPSRIQ LSNDNEL
//