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A7ZYN8 (SSUD_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:EcHS_A1044
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [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-Rule MF_01229

Catalytic activity

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01229

Miscellaneous

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

Sequence similarities

Belongs to the SsuD family.

Ontologies

Keywords
   LigandFlavoprotein
FMN
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functionalkanesulfonate monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Alkanesulfonate monooxygenase HAMAP-Rule MF_01229
PRO_1000066820

Sequences

Sequence LengthMass (Da)Tools
A7ZYN8 [UniParc].

Last modified October 23, 2007. 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 pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV05392.1.
RefSeqYP_001457775.1. NC_009800.1.

3D structure databases

ProteinModelPortalA7ZYN8.
SMRA7ZYN8. Positions 1-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A1044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV05392; ABV05392; EcHS_A1044.
GeneID5591079.
KEGGecx:EcHS_A1044.
PATRIC18312072. VBIEscCol77814_1013.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2141.
HOGENOMHOG000134568.
KOK04091.
OMAREVRFGI.
OrthoDBEOG62NX1P.
ProtClustDBPRK00719.

Enzyme and pathway databases

BioCycECOL331112:GHHI-1038-MONOMER.

Family and domain databases

Gene3D3.20.20.30. 2 hits.
HAMAPMF_01229. Alkanesulf_monooxygen.
InterProIPR019911. Alkanesulphonate_mOase_FMN-dep.
IPR011251. Luciferase-like_dom.
[Graphical view]
PfamPF00296. Bac_luciferase. 1 hit.
[Graphical view]
SUPFAMSSF51679. SSF51679. 1 hit.
TIGRFAMsTIGR03565. alk_sulf_monoox. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSSUD_ECOHS
AccessionPrimary (citable) accession number: A7ZYN8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 48 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