ID   OXLA_NEUCR              Reviewed;         696 AA.
AC   P23623; Q7RVE5; Q8X0D4;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   Flags: Precursor;
GN   Name=lox; ORFNames=B14A6.230, NCU01066;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=2145270; DOI=10.1016/s0021-9258(17)44895-2;
RA   Niedermann D.M., Lerch K.;
RT   "Molecular cloning of the L-amino-acid oxidase gene from Neurospora
RT   crassa.";
RL   J. Biol. Chem. 265:17246-17251(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- INDUCTION: By addition of L-amino acids after nitrogen starvation, by
CC       starvation in phosphate buffer and by the addition of protein synthesis
CC       inhibitors, D-amino acids, or ATP.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AL670007; CAD21325.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32442.1; -; Genomic_DNA.
DR   PIR; A38314; A38314.
DR   RefSeq; XP_961678.1; XM_956585.2.
DR   AlphaFoldDB; P23623; -.
DR   SMR; P23623; -.
DR   STRING; 367110.P23623; -.
DR   PaxDb; 5141-EFNCRP00000004415; -.
DR   EnsemblFungi; EAA32442; EAA32442; NCU01066.
DR   GeneID; 3877869; -.
DR   KEGG; ncr:NCU01066; -.
DR   VEuPathDB; FungiDB:NCU01066; -.
DR   HOGENOM; CLU_004498_8_2_1; -.
DR   InParanoid; P23623; -.
DR   OMA; NCSHLMS; -.
DR   OrthoDB; 3597164at2759; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR   GO; GO:0009063; P:amino acid catabolic process; IBA:GO_Central.
DR   Gene3D; 1.20.1440.240; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
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   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW   Reference proteome; Zymogen.
FT   PROPEP          1..130
FT                   /id="PRO_0000001708"
FT   CHAIN           131..696
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000001709"
FT   BINDING         207
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         564
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         649
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         658..661
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        6..13
FT                   /note="AAGAALLA -> RGCGTAR (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="F -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391..414
FT                   /note="SASAHSYWDTLYEGMYFSASTWKT -> APALTRTGTRCTKGCTFPRRRGA
FT                   (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="V -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        684..685
FT                   /note="AT -> GRP (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   696 AA;  77013 MW;  3909C59198E96008 CRC64;
     MKWSAAAGAA LLALPANSAV TASLPLKLET RSSLNSRLSN IHVERSASVE GAISYTYGSC
     QAKREEEAHH SISQPTDAHH DRLVWVIPEN VQSGGCISAW SRANGRLVGR SRPQSFDFKS
     IKMRRDLKAR ATKPSDSVAI HMTTDNGINP WGPWFDGVKL LEDKEISTVD VEKAKSKNIA
     IVGAGMSGLM TYLCLTQAGM TNVSIIEGGN RLGGRVHTEY LSGGPFDYSY QEMGPMRFPN
     TITLGNETYN VSDHQLVFQL AEEMNSLNGH SKNLSVDFIP WYQSNSNGLY YYDGIKNPET
     GLPPTLAELA ANSSLALTRV SNNSTKSLSQ KVDAFLPDTD KFFAEMAQNM FKAHADWLSG
     GLAGLPGDQW SEFGFMVNYL RGSLNDTAFL SASAHSYWDT LYEGMYFSAS TWKTIDGGLN
     RLPLSFHPLV DNATTLNRRV ERVAFDAETQ KVTLHSRNSY KDSFESSEHD YAVIAAPFSI
     VKKWRFSPAL DLTAPTLANA IQNLEYTSAC KVALEFRTRF WEHLPQPIYG SCSTTSDIPG
     IGSICYPSYN INGTDGPASI LASYISGADW GDRWVSTPEE EHVQYVLNAM AEIHGEELVK
     EQYTGQFNRR CWALDPLESA SWASPTVGQH ELYLPEYFQT RNNLVFVGEH TSYTHAWIAS
     ALESGIRGSV QLLLELGLVD EAKATVDKWM ARWIDV
//