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Reviewed, UniProtKB/Swiss-Prot Q9HYG2 (SSUD_PSEAE)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alkanesulfonate monooxygenase
    EC=1.14.14.5
Alternative name(s):
    FMNH2-dependent aliphatic sulfonate monooxygenase
    PA13
Gene names
Name: ssuD
Ordered Locus Names: PA3444
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the desulfonation of aliphatic sulfonates By similarity.

Catalytic activity

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

Induction

Repressed by sulfate, cysteine, or thiocyanate. HAMAP 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
   LigandFMN
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalkanesulfonate monooxygenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 382381Alkanesulfonate monooxygenase HAMAP MF_01229
PRO_0000216711

Experimental info

Sequence conflict71W → A AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9HYG2-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BF2C6EE4A1E102CD

FASTA38241,567
        10         20         30         40         50         60 
MSLEIFWFLP THGDGHYLGT TQGARAVDHG YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL 

        70         80         90        100        110        120 
VAASLIPVTQ RLKFLVALRP GIISPTVAAR QAATLDRLSN GRALFNLVTG GDPDELAGDG 

       130        140        150        160        170        180 
LHLSHAERYE ASVEFTRIWR RVLEGETVDY AGKHIQVKGA KLLYPPLQQP RPPLYFGGSS 

       190        200        210        220        230        240 
EAAQDLAAEQ VELYLTWGEP PAAVAEKIAQ VREKAARQGR QVRFGIRLHV IVRETSEEAW 

       250        260        270        280        290        300 
QAADRLIAHL DDDTIARAQA SLARFDSVGQ QRMAALHGGS RDNLEVSPNL WAGVGLVRGG 

       310        320        330        340        350        360 
AGTALVGDGP TVAARVREYA ELGIDTFIFS GYPHLEESYR VAELLFPHLD VQRPAQPEGR 

       370        380 
GYVSPFGEMV ANDILPRQAA QS 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Regulation of the sulfate starvation response in Pseudomonas aeruginosa: role of cysteine biosynthetic intermediates."
Hummerjohann J., Kuttel E., Quadroni M., Ragaller J., Leisinger T., Kertesz M.A.
Microbiology 144:1375-1386(1998) [PubMed: 9611812] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

AE004091 Genomic DNA. Translation: AAG06832.1.
PIRA83215.
RefSeqNP_252134.1.

3D structure databases

HSSPHSSP built from PDB template 1M41 based on UniProtKB P80645.
SMRQ9HYG2. Positions 1-358.
ModBaseSearch...

Genome annotation databases

GeneID879163.
GenomeReviewsGene locus PA3444 in contig AE004091_GR.
KEGGpae:PA3444.

Organism-specific databases

PseudoCAPPA3444.
CMRSearch...

Phylogenomic databases

HOGENOMQ9HYG2.
OMAQ9HYG2. NIFWFLP.

Enzyme and pathway databases

BioCycPAER208964:PA3444-MON.
BRENDA1.14.14.5. 354.

Family and domain databases

HAMAPMF_01229.
[Tree]
InterProIPR019911. Alkanesulfonate_mOase_FMN-dep.
IPR016048. Luciferase-like_sub.
[Graphical view]
PfamPF00296. Bac_luciferase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03565. Alk_sulf_monoox. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSSUD_PSEAE
AccessionPrimary (citable) accession number: Q9HYG2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 43 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents