ID   YOBN_BACSU              Reviewed;         478 AA.
AC   O34363; Q796E0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 3.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Putative L-amino-acid oxidase YobN;
DE            EC=1.4.3.2;
GN   Name=yobN; OrderedLocusNames=BSU19020;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB84430.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF027868; AAB84430.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB13794.2; -; Genomic_DNA.
DR   PIR; E69899; E69899.
DR   RefSeq; NP_389783.1; NC_000964.3.
DR   AlphaFoldDB; O34363; -.
DR   SMR; O34363; -.
DR   STRING; 224308.BSU19020; -.
DR   PaxDb; 224308-BSU19020; -.
DR   EnsemblBacteria; CAB13794; CAB13794; BSU_19020.
DR   GeneID; 939632; -.
DR   KEGG; bsu:BSU19020; -.
DR   eggNOG; COG1231; Bacteria.
DR   InParanoid; O34363; -.
DR   OrthoDB; 25353at2; -.
DR   BioCyc; BSUB:BSU19020-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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; 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:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 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   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..478
FT                   /note="Putative L-amino-acid oxidase YobN"
FT                   /id="PRO_0000359955"
FT   BINDING         34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..81
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         460..463
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54055 MW;  29131507CD3F7DC9 CRC64;
     MNSLMNDDMV KIIRNGLSAS QHPKHILVIG AGLSGLVSAS LLKNAGHRVT ILEASGRAGG
     RVCTLRSPFS DDLYFNAGPM RIPNNHSLTL EYIKKFKLPT NVFINRTPMD IIYANGIKTR
     LQVFERAPGI LRYPVAPNEQ GKTSEELMLS LLQPILNFIN QNPARNWRIV EEQYKNHSLS
     SFLNTYFSYG AIDMIGVLLD MEAYMGMSLV EVLRESIFFS SPAHFYEITG GMDLLPHAFL
     PQLKTNILYH QKMMKMSQGE NRVTIHCQHQ QTAEFTSFTA DLAIVTIPFS TLRFVKVEPY
     HSFSYYKRRA IRELNYISAT KIGIEFKSRF WEKAGQHGGK SITDLPIRFS YYPSRNIGAN
     GHAVILASYT WADEALIWDS LSEGERIQYT LLNLSEIYGD IVWSEFVSGT SFSWSQYPYS
     AGGFTAFEPG QELELYPYIP VPEGRVHFAG EHASLTHAWM QGAIESGIRV AYEVNRLP
//