Skip Header

Contribute Send feedback
Read comments (?) or add your own

O34974 (MOXC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 monooxygenase moxC
EC=1.14.-.-
Gene names
Name:moxC
Synonyms:ytnJ
Ordered Locus Names:BSU29310
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in methionine degradation. May play a role in a sulfur salvage pathway. Ref.3

Cofactor

FMN.

Subunit structure

Homodimer Probable. Ref.4

Induction

Induced when methionine is the sulfur source, but not by sulfate. Ref.5

Disruption phenotype

Reduced growth with methionine or methionine sulfoxide as unique source of sulfur. Ref.3

Sequence similarities

Belongs to the ntaA/snaA/soxA(dszA) monooxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Putative monooxygenase moxC
PRO_0000360622

Regions

Nucleotide binding145 – 1495FMN binding
Nucleotide binding217 – 2204FMN binding

Sites

Binding site581FMN; via amide nitrogen and carbonyl oxygen
Binding site951FMN

Secondary structure

1 .......................................... 442
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34974 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8C9D72FEB983FBF5

FASTA44249,411
        10         20         30         40         50         60 
MTRADFIQFG AMIHGVGGTT DGWRHPDVDP SASTNIEFYM KKAQTAEKGL FSFIFIADGL 

        70         80         90        100        110        120 
FISEKSIPHF LNRFEPITIL SALASVTKNI GLVGTFSTSF TEPFTISRQL MSLDHISGGR 

       130        140        150        160        170        180 
AGWNLVTSPQ EGAARNHSKS NLPEHTERYE IAQEHLDVVR GLWNSWEHDA FIHNKKTGQF 

       190        200        210        220        230        240 
FDQAKLHRLN HKGKYFQVEG PLNIGRSKQG EPVVFQAGSS ETGRQFAAKN ADAIFTHSNS 

       250        260        270        280        290        300 
LEETKAFYAD VKSRAADEGR DPSSVRIFPG ISPIVADTEE EAEKKYREFA ELIPIENAVT 

       310        320        330        340        350        360 
YLARFFDDYD LSVYPLDEPF PDIGDVGKNA FQSTTDRIKR EAKARNLTLR EVAQEMAFPR 

       370        380        390        400        410        420 
TLFIGTPERV ASLIETWFNA EAADGFIVGS DIPGTLDAFV EKVIPILQER GLYRQDYRGG 

       430        440 
TLRENLGLGI PQHQSVLHSS HH

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Extracting biological information from DNA arrays: an unexpected link between arginine and methionine metabolism in Bacillus subtilis."
Sekowska A., Robin S., Daudin J.-J., Henaut A., Danchin A.
Genome Biol. 2:RESEARCH0019.1-RESEARCH0019.12(2001) [PubMed: 11423008] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
Strain: 168.
[4]"Structure of ytnj from bacillus subtilis."
New York structural genomix research consortium (NYSGXRC)
Submitted (MAR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.
[5]"Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism."
Burguiere P., Fert J., Guillouard I., Auger S., Danchin A., Martin-Verstraete I.
J. Bacteriol. 187:6019-6030(2005) [PubMed: 16109943] [Abstract]
Cited for: INDUCTION BY METHIONINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF008220 Genomic DNA. Translation: AAC00332.1.
AL009126 Genomic DNA. Translation: CAB14891.1.
PIRE69997.
RefSeqNP_390809.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TVLX-ray2.10A2-442[»]
1YW1X-ray2.81A1-442[»]
ProteinModelPortalO34974.
SMRO34974. Positions 3-431.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002474; EBBACP00000002474; EBBACG00000002469.
GeneID937365.
GenomeReviewsGene locus BSU29310 in contig AL009126_GR.
KEGGbsu:BSU29310.
NMPDRfig|224308.1.peg.2934.
PATRIC18977762. VBIBacSub10457_3069.

Organism-specific databases

GenoListBSU29310. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002161.
HOGENOMHBG673014.
OMANNFRATT.
PhylomeDBO34974.
ProtClustDBCLSK887711.

Enzyme and pathway databases

BioCycBSUB:BSU29310-MONOMER.

Family and domain databases

InterProIPR011251. Luciferase-like_dom.
IPR016215. NTA_MOA.
[Graphical view]
Gene3DG3DSA:3.20.20.30. Luciferase_like. 2 hits.
PfamPF00296. Bac_luciferase. 1 hit.
[Graphical view]
PIRSFPIRSF000337. NTA_MOA. 1 hit.
SUPFAMSSF51679. Luciferase_like. 1 hit.
TIGRFAMsTIGR03860. FMN_nitrolo. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMOXC_BACSU
AccessionPrimary (citable) accession number: O34974
Secondary accession number(s): Q795U8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 66 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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