YOBN_BACSU
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 03-AUG-2022, entry version 114.
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; Firmicutes; 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; O34363; -.
DR EnsemblBacteria; CAB13794; CAB13794; BSU_19020.
DR GeneID; 939632; -.
DR KEGG; bsu:BSU19020; -.
DR eggNOG; COG1231; Bacteria.
DR InParanoid; O34363; -.
DR OMA; YTHAWIA; -.
DR BioCyc; BSUB:BSU19020-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 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