Skip Header

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

P80645 (SSUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 105. 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:
Alkanesulfonate monooxygenase
EC=1.14.14.5
Alternative name(s):
FMNH2-dependent aliphatic sulfonate monooxygenase
Sulfate starvation-induced protein 6
Short name=SSI6
Gene names
Name:ssuD
Synonyms:ycbN
Ordered Locus Names:b0935, JW0918
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in desulfonation of aliphatic sulfonates. Catalyzes the conversion of pentanesulfonic acid to sulfite and pentaldehyde and is able to desulfonate a wide range of sulfonated substrates including C-2 to C-10 unsubstituted linear alkanesulfonates, substituted ethanesulfonic acids and sulfonated buffers. 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.

Induction

Repressed by sulfate or cysteine. HAMAP MF_01229

Miscellaneous

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

Sequence similarities

Belongs to the SsuD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 381380Alkanesulfonate monooxygenase HAMAP MF_01229
PRO_0000216706

Natural variations

Natural variant2981R → C in strain: K12 / MC4100; inactive.

Experimental info

Mutagenesis2981R → C: Loss of activity. Ref.6
Sequence conflict191G → Q AA sequence Ref.5

Secondary structure

1 ........................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80645 [UniParc].

Last modified January 23, 2007. Version 3.
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

« Hide 'large scale' references
[1]"The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl."
Van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M.M., Leisinger T.
J. Biol. Chem. 274:29358-29365(1999) [PubMed: 10506196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli."
Quadroni M., Staudenmann W., Kertesz M.A., James P.
Eur. J. Biochem. 239:773-781(1996) [PubMed: 8774726] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[6]"Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli."
Eichhorn E., van der Ploeg J.R., Leisinger T.
J. Biol. Chem. 274:26639-26646(1999) [PubMed: 10480865] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF ARG-298.
[7]"Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD."
Eichhorn E., Davey C.A., Sargent D.F., Leisinger T., Richmond T.J.
J. Mol. Biol. 324:457-468(2002) [PubMed: 12445781] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ237695 Genomic DNA. Translation: CAB40391.1.
U00096 Genomic DNA. Translation: AAC74021.1.
AP009048 Genomic DNA. Translation: BAA35690.1.
PIRF64833.
RefSeqNP_415455.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M41X-ray2.30A/B2-381[»]
1NQKX-ray2.20A1-381[»]
ProteinModelPortalP80645.
SMRP80645. Positions 1-362.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10928N.
IntActP80645. 8 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003023; EBESCP00000003023; EBESCG00000002479.
EBESCT00000017948; EBESCP00000017239; EBESCG00000017004.
GeneID945557.
GenomeReviewsGene locus JW0918 in contig AP009048_GR.
Gene locus b0935 in contig U00096_GR.
KEGGecj:JW0918.
eco:b0935.
PATRIC32117089. VBIEscCol129921_0969.

Organism-specific databases

EchoBASEEB3470.
EcoGeneEG13706. ssuD.

Phylogenomic databases

eggNOGCOG2141.
GeneTreeEBGT00050000008394.
HOGENOMHBG639644.
OMASLEGKHI.
PhylomeDBP80645.
ProtClustDBPRK00719.

Enzyme and pathway databases

BioCycEcoCyc:MONOMER-162.
MetaCyc:MONOMER-162.

Gene expression databases

GenevestigatorP80645.

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_ECOLI
AccessionPrimary (citable) accession number: P80645
Secondary accession number(s): P75852, Q9RM46
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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