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B1X8N9 (SSUD_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Alkanesulfonate monooxygenase

EC=1.14.14.5
Alternative name(s):
FMNH2-dependent aliphatic sulfonate monooxygenase
Gene names
Name:ssuD
Ordered Locus Names:ECDH10B_1005
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length381 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

Subunit structure

Homotetramer By similarity. HAMAP MF_01229

Miscellaneous

FMNH2 which is absolutely required for this enzymatic reaction, is provided by SsuE By similarity. HAMAP MF_01229

Sequence similarities

Belongs to the SsuD family.

Ontologies

Keywords
   LigandFMN
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionalkanesulfonate monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Alkanesulfonate monooxygenase HAMAP MF_01229
PRO_1000139620

Sequences

Sequence LengthMass (Da)Tools
B1X8N9 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 4D05E510487999C6

FASTA38141,736
        10         20         30         40         50         60 
MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL 

        70         80         90        100        110        120 
VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG 

       130        140        150        160        170        180 
VFLDHSERYE ASAEFTQVWR RLLQRETVDF NGKHIHVRGA KLLFPAIQQP YPPLYFGGSS 

       190        200        210        220        230        240 
DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW 

       250        260        270        280        290        300 
QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG 

       310        320        330        340        350        360 
AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPLLD VAIPEIPQPQ 

       370        380 
PLNPQGEAVA NDFIPRKVAQ S 

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000948 Genomic DNA. Translation: ACB02135.1.
RefSeqYP_001729913.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1X8N9.
SMRB1X8N9. Positions 1-362.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1X8N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000011670; EBESCP00000011198; EBESCG00000010732.
GeneID6060526.
GenomeReviewsGene locus ECDH10B_1005 in contig CP000948_GR.
KEGGecd:ECDH10B_1005.
PATRIC18461838. VBIEscCol59506_1020.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008394.
HOGENOMHBG639644.
OMASLEGKHI.
ProtClustDBPRK00719.

Enzyme and pathway databases

BioCycECOL316385:ECDH10B_1005-MONOMER.

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 nameSSUD_ECODH
AccessionPrimary (citable) accession number: B1X8N9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families