ID OXLA_CRODM Reviewed; 498 AA. AC K9N7B7; DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2013, sequence version 1. DT 12-APR-2017, entry version 13. DE RecName: Full=L-amino acid oxidase Cdc18 {ECO:0000303|PubMed:19863078}; DE AltName: Full=CdcLAAO; DE Short=LAO; DE EC=1.4.3.2 {ECO:0000269|PubMed:23287728}; DE Flags: Precursor; Fragment; OS Crotalus durissus cumanensis (South American rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=184542 {ECO:0000312|EMBL:AFY13334.1}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RC TISSUE=Venom, and Venom gland; RX PubMed=23287728; DOI=10.1016/j.toxicon.2012.11.027; RA Vargas L.J., Quintana J.C., Pereanez J.A., Nunez V., Sanz L., RA Calvete J.J.; RT "Cloning and characterization of an antibacterial L-amino acid oxidase RT from Crotalus durissus cumanensis venom."; RL Toxicon 64:1-11(2013). RN [2] RP PROTEIN SEQUENCE OF 3-17, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=19863078; DOI=10.1021/pr9008749; RA Calvete J.J., Sanz L., Cid P., de la Torre P., Flores-Diaz M., RA Dos Santos M.C., Borges A., Bremo A., Angulo Y., Lomonte B., RA Alape-Giron A., Gutierrez J.M.; RT "Snake venomics of the Central American rattlesnake Crotalus simus and RT the South American Crotalus durissus complex points to neurotoxicity RT as an adaptive paedomorphic trend along Crotalus dispersal in South RT America."; RL J. Proteome Res. 9:528-544(2010). CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly CC hydrophobic and aromatic L-amino acids (tested on L-Leu), thus CC producing hydrogen peroxide that may contribute to the diverse CC toxic effects of this enzyme. Damages cell membranes of the Gram- CC positive bacteria S.aureus (MIC=8 ug/ml and MBC=16 ug/ml) and the CC Gram-negative bacteria A.baumannii (MIC=16 ug/ml and MBC=32 CC ug/ml). This antimicrobial activity is dependent on the production CC of hydrogen peroxyde, since it is inhibited by catalase, a CC hydrogen peroxyde scavenger. {ECO:0000269|PubMed:23287728}. CC -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid CC + NH(3) + H(2)O(2). {ECO:0000269|PubMed:23287728}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=9.23 uM for L-Leu {ECO:0000269|PubMed:23287728}; CC Vmax=0.46 uM/min/mg enzyme for L-Leu CC {ECO:0000269|PubMed:23287728}; CC -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:23287728}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23287728}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}. CC -!- MISCELLANEOUS: Does not show antimicrobial activities against CC E.coli. Does not induce cytotoxicity toward C2C12 cells (at 40 CC ug/ml) and peripheral blood mononuclear cells (up to 200 ug/ml). CC {ECO:0000269|PubMed:23287728}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. {ECO:0000250|UniProtKB:P56742}. 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; KC154267; AFY13334.1; -; mRNA. DR ProteinModelPortal; K9N7B7; -. DR SMR; K9N7B7; -. 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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01593; Amino_oxidase; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond; KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal. FT SIGNAL <1 2 {ECO:0000269|PubMed:19863078}. FT CHAIN 3 498 L-amino acid oxidase Cdc18. FT /FTId=PRO_0000430748. FT NP_BIND 45 46 FAD. {ECO:0000250|UniProtKB:P81382}. FT NP_BIND 65 66 FAD. {ECO:0000250|UniProtKB:P81382}. FT NP_BIND 87 90 FAD. {ECO:0000250|UniProtKB:P81382}. FT NP_BIND 466 471 FAD. {ECO:0000250|UniProtKB:P81382}. FT REGION 466 467 Substrate binding. FT {ECO:0000250|UniProtKB:P81382}. FT BINDING 73 73 FAD. {ECO:0000250|UniProtKB:P81382}. FT BINDING 90 90 Substrate. FT {ECO:0000250|UniProtKB:P81382}. FT BINDING 223 223 Substrate. FT {ECO:0000250|UniProtKB:P81382}. FT BINDING 263 263 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250|UniProtKB:P81382}. FT BINDING 374 374 Substrate. FT {ECO:0000250|UniProtKB:P81382}. FT BINDING 459 459 FAD. {ECO:0000250|UniProtKB:P81382}. FT CARBOHYD 363 363 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT DISULFID 12 173 {ECO:0000250|UniProtKB:P81382}. FT DISULFID 333 414 {ECO:0000250|UniProtKB:P81382}. FT NON_TER 1 1 {ECO:0000312|EMBL:AFY13334.1}. SQ SEQUENCE 498 AA; 56827 MW; 766AD523DD75FF5B CRC64; SCADDRNPLE ECFRETDYEE FLEIARNGLT VTSNPKHVVI VGAGMAGLSA AYVLAGAGHQ VTVLEASERV GGRVRTYRKK DWYANLGPMR LPTKHRIVRE YIRKFGLQLN EFFQENENAW YFIKNIRKRV REVKNNPGIL EYPVKPSEEG KSAAQLYVES LRKVVKELKR TNCKYILDKY DTYSTKEYLL KEGNLSPGAV DMIGDLLNED SGYYVSFIES LKHDDIFGYE KRFDEIVGGM DQLPTSMYEA IKEKVQVHFN ARVIEIQQND RETKVTYQTS ANEMPSVTAD YVIVCTTSRA ARRIKFEPPL PPKKAHALRS VHYRSGTKIF LTCKRKFWED DGIRGGKSTT DLPSRFIYYP NHNFTSGVGV IIAYGIGDDA NFFQALDFKD CADIVINDLS LIHQLPKEDI QTFCRPSMIQ RWSLDKYAMG GITTFTPYQF QHFSEALTAP FKRIYFAGEY TAQFHGWIDS TIKSGLTAAR DVNRASENPS GIHLSNDN //