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O34363 (YOBN_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative L-amino-acid oxidase YobN
EC=1.4.3.2
Gene names
Name:yobN
Ordered Locus Names:BSU19020
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD By similarity.

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence caution

The sequence AAB84430.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB13794.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-amino-acid oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Putative L-amino-acid oxidase YobN
PRO_0000359955

Regions

Transmembrane22 – 3817Helical; Potential
Nucleotide binding76 – 772FAD By similarity
Nucleotide binding456 – 4594FAD By similarity

Sites

Binding site301FAD By similarity
Binding site491FAD By similarity
Binding site571FAD By similarity
Binding site771Substrate By similarity
Binding site3651Substrate By similarity
Binding site4471FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
O34363 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 9555473E8D279BAE

FASTA47453,627
        10         20         30         40         50         60 
MNDDMVKIIR NGLSASQHPK HILVIGAGMS GLVSASLLKN AGHRVTILEA SGRAGGRVCT 

        70         80         90        100        110        120 
LRSPFSDDLY FNAGPMRIPN NHSLTLEYIK KFKLPTNVFI NRTPMDIIYA NGIKTRLQVF 

       130        140        150        160        170        180 
ERAPGILRYP VAPNEQGKTS EELMLSLLQP ILNFINQNPA RNWRIVEEQY KNHSLSSFLN 

       190        200        210        220        230        240 
TYFSYGAIDM IGVLLDMEAY MGMSLVEVLR ESIFFSSPAH FYEITGGMDL LPHAFLPQLK 

       250        260        270        280        290        300 
TNILYHQKMM KMSQGENRVT IHCQHQQTAE FTSFTADLAI VTIPFSTLRF VKVEPYHSFS 

       310        320        330        340        350        360 
YYKRRAIREL NYISATKIGI EFKSRFWEKA GQHGGKSITD LPIRFSYYPS RNIGANGHAV 

       370        380        390        400        410        420 
ILASYTWADE ALIWDSLSEG ERIQYTLLNL SEIYGDIVWS EFVSGTSFSW SQYPYSAGGF 

       430        440        450        460        470 
TAFEPGQELE LYPYIPVPEG RVHFAGEHAS LTHAWMQGAI ESGIRVAYEV NRLP

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF027868 Genomic DNA. Translation: AAB84430.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB13794.1. Different initiation.
PIRE69899.

3D structure databases

HSSPHSSP built from PDB template 1F8R based on UniProtKB P81382.
ProteinModelPortalO34363.
SMRO34363. Positions 3-474.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU19020.

Proteomic databases

PaxDbO34363.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13794; CAB13794; BSU19020.
KEGGbsu:BSU19020.
PATRIC18975649. VBIBacSub10457_2015.

Organism-specific databases

GenoListBSU19020.

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000088141.
ProtClustDBCLSK887401.

Enzyme and pathway databases

BioCycBSUB:BSU19020-MONOMER.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameYOBN_BACSU
AccessionPrimary (citable) accession number: O34363
Secondary accession number(s): Q796E0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents