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A7GQ63 (A7GQ63_BACCN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alkanesulfonate monooxygenase HAMAP MF_01229

EC=1.14.14.5 HAMAP MF_01229
Alternative name(s):
FMNH2-dependent aliphatic sulfonate monooxygenase HAMAP MF_01229
Gene names
Name:ssuD HAMAP MF_01229
Ordered Locus Names:Bcer98_1997
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP] EMBL ABS22271.1
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the desulfonation of aliphatic sulfonates By similarity. HAMAP MF_01229

Catalytic activity

An alkanesufonate (R-CH(2)-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) + FMN + sulfite + H2O. HAMAP MF_01229

Sequence similarities

Belongs to the SsuD family. HAMAP MF_01229

Ontologies

Sequences

Sequence LengthMass (Da)Tools
A7GQ63 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 48F3F05EF1BC082F

FASTA37141,045
        10         20         30         40         50         60 
MEILWFIPAY GDGRYLGTTK RGRAAEYGYY KQVAQAADYL GYSGVLLPTG QGCEDPWVLA 

        70         80         90        100        110        120 
SALAAETEKL RFLVAVRPGI MSPTVAARMA STFDRISDGR LLINVVAGGD PVELQGDGLF 

       130        140        150        160        170        180 
LDHDARYDAT DEFLKVWKSV LQGEQVSLEG EYIQVKDSKV VFPPVQSPHP PIYFGGSSDA 

       190        200        210        220        230        240 
GKAVAAEHCD VYLTWGEQPA QVEQKIKEVK KLAEAKGRTV RFGIRLHVIV RETEEEAWKD 

       250        260        270        280        290        300 
AERCIQYVDD ATIELAQKTF ARYESVGQKR MTRLNKGTRE ALEISPNLWA GIGLIRGGAG 

       310        320        330        340        350        360 
TALVGDPHTV AKRIKEYEEL GIDTFILSGY PHLEEAYQVA ELLFPLLPVS QNEKDKIVGE 

       370 
MIADAYALEK K 

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References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS22271.1.
RefSeqYP_001375266.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GQ63.
SMRA7GQ63. Positions 1-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GQ63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000037853; EBBACP00000036904; EBBACG00000037844.
GeneID5345271.
GenomeReviewsGene locus Bcer98_1997 in contig CP000764_GR.
KEGGbcy:Bcer98_1997.
PATRIC18932544. VBIBacCyt128034_2116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2141.
GeneTreeEBGT00050000002162.
HOGENOMHBG639644.
OMASLEGKHI.
ProtClustDBPRK00719.

Family and domain databases

HAMAPMF_01229. Alkanesulf_monooxygen.
[Tree]
InterProIPR019911. Alkanesulphonate_mOase_FMN-dep.
IPR011251. Luciferase-like_dom.
[Graphical view]
Gene3DG3DSA:3.20.20.30. Luciferase_like. 2 hits.
KOK04091.
PfamPF00296. Bac_luciferase. 1 hit.
[Graphical view]
SUPFAMSSF51679. Luciferase_like. 1 hit.
TIGRFAMsTIGR03565. Alk_sulf_monoox. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA7GQ63_BACCN
AccessionPrimary (citable) accession number: A7GQ63
Entry history
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)