Alkanesulfonate monooxygenase (P80645)

Identification
Name:Alkanesulfonate monooxygenase
Synonyms:
  • FMNH2-dependent aliphatic sulfonate monooxygenase
  • Sulfate starvation-induced protein 6
  • SSI6
Gene Name:ssuD
Enzyme Class:
Biological Properties
General Function:Involved in alkanesulfonate monooxygenase activity
Specific 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Alkanesulfonate + 1.0FMNH + 1.0Oxygen ↔ 1.0Aldehyde + 1.0Flavin Mononucleotide + 1.0Sulfite + 1.0Water
ReactionCard
SMPDB Reactions:
1.0alkylsulfonate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Sulfite+1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0alkylsulfonate + 1.0FMNH2 + 1.0Oxygen → 1.0Betaine aldehyde + 1.0Sulfite + 1.0Flavin Mononucleotide + 1.0Water + 2.0Hydrogen ion + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Sulfite+1.0Thumb+1.0Thumb+1.0Thumb
1.0Butanesulfonate + 1.0Oxygen + 1.0FMNH2 → 1.0Hydrogen ion + 1.0Water + 1.0Sulfite + 1.0Flavin Mononucleotide + 1.0Betaine aldehyde + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Sulfite+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Oxygen + 1.0FMNH2 + 1.03-(N-morpholino)propanesulfonate → 1.0Sulfite + 1.0Water + 1.0Hydrogen ion + 1.0Flavin Mononucleotide + 1.0Betaine aldehyde + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Sulfite+1.0Thumb+1.0Thumb
1.0 ethanesulfonate + 1.0Oxygen + 1.0FMNH2 → 1.0Hydrogen ion + 1.0Water + 1.0Flavin Mononucleotide + 1.0Sulfite + 1.0Betaine aldehyde + 1.0Sulfite
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Sulfite+1.0Thumb
1.0 isethionate + 1.0Oxygen + 1.0FMNH2 → 1.0Betaine aldehyde + 1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite + 1.0Sulfite
ReactionCard
1.0Thumb+1.0methanesulfonate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Sulfite+1.0Thumb+1.0Thumb
1.0Oxygen + 1.0methanesulfonate + 1.0FMNH2 + 1.0Methanesulfonate → 1.0Hydrogen ion + 1.0Water + 1.0Flavin Mononucleotide + 1.0Sulfite + 1.0Betaine aldehyde + 1.0Sulfite
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0FMNH + 1.0Isethionic acid + 1.0Oxygen → 1.0Flavin Mononucleotide + 1.0Glycolaldehyde + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Butanesulfonate + 1.0FMNH + 1.0Oxygen → 1.0Butanal + 1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0FMNH + 1.0Oxygen + 1.0Sulfoacetate → 1.0Flavin Mononucleotide + 1.0Glyoxylic acid + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0FMNH + 1.0Methanesulfonate + 1.0Oxygen → 1.0Formaldehyde + 1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Ethanesulfonate + 1.0FMNH + 1.0Oxygen → 1.0Acetaldehyde + 1.0Flavin Mononucleotide + 1.0Hydrogen ion + 1.0Water + 1.0Sulfite
ReactionCard
1.0An alkanesufonate (R-CH(2)-SO(3)H)+1.0Thumb+1.0Thumb → 1.0an aldehyde (R-CHO)+1.0Thumb+1.0Thumb+1.0Thumb
1.0An alkanesufonate (R-CH(2)-SO(3)H) + 1.0FMNH(2) + 1.0Oxygen → 1.0an aldehyde (R-CHO) + 1.0Flavin Mononucleotide + 1.0Sulfite + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24254 ethanesulfonateMetaboCard
ECMDB24255 isethionateMetaboCard
ECMDB242533-(N-morpholino)propanesulfonateMetaboCard
ECMDB00990AcetaldehydeMetaboCard
ECMDB21646AldehydeMetaboCard
ECMDB23762AlkanesulfonateMetaboCard
ECMDB01252Betaine aldehydeMetaboCard
ECMDB03543ButanalMetaboCard
ECMDB21313ButanesulfonateMetaboCard
ECMDB21330EthanesulfonateMetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB01142FMNHMetaboCard
ECMDB23187FMNH(2)MetaboCard
ECMDB24059FMNH2MetaboCard
ECMDB01426FormaldehydeMetaboCard
ECMDB02165GlycolaldehydeMetaboCard
ECMDB00119Glyoxylic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21233Isethionic acidMetaboCard
ECMDB21344MethanesulfonateMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB21358SulfoacetateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b0935
Gene OrientationCounterclockwise
Centisome Percentage:21.43
Left Sequence End994066
Right Sequence End995211
Gene Sequence:
>1146 bp
ATGAGTCTGAATATGTTCTGGTTTTTACCGACCCACGGTGACGGGCATTATCTGGGAACG
GAAGAAGGTTCACGCCCGGTTGATCACGGTTATCTGCAACAAATTGCGCAAGCGGCGGAT
CGTCTTGGCTATACCGGTGTGCTAATTCCAACGGGGCGCTCCTGCGAAGATGCGTGGCTG
GTTGCCGCATCGATGATCCCGGTGACGCAGCGGCTGAAGTTTCTTGTCGCCCTGCGTCCC
AGCGTAACCTCACCTACCGTTGCCGCCCGCCAGGCCGCCACGCTTGACCGTCTCTCAAAT
GGACGTGCGTTGTTTAACCTGGTCACAGGCAGCGATCCACAAGAGCTGGCAGGCGACGGA
GTGTTCCTTGATCATAGCGAGCGCTACGAAGCCTCGGCGGAATTTACCCAGGTCTGGCGG
CGTTTATTGCAGAGAGAAACCGTCGATTTCAACGGTAAACATATTCATGTGCGCGGAGCA
AAACTGCTCTTCCCGGCGATTCAACAGCCGTATCCGCCACTTTACTTTGGCGGATCGTCA
GATGTCGCCCAGGAGCTGGCGGCAGAACAGGTTGATCTCTACCTCACCTGGGGCGAACCG
CCGGAACTGGTTAAAGAGAAAATCGAACAAGTGCGGGCGAAAGCTGCCGCGCATGGACGC
AAAATTCGTTTCGGTATTCGTCTGCATGTGATTGTTCGTGAAACTAACGACGAAGCGTGG
CAGGCCGCCGAGCGGTTAATCTCGCATCTTGATGATGAAACTATCGCCAAAGCACAGGCC
GCATTCGCCCGGACGGATTCCGTAGGGCAACAGCGAATGGCGGCGTTACATAACGGCAAG
CGCGACAATCTGGAGATCAGCCCCAATTTATGGGCGGGCGTTGGCTTAGTGTGCGGCGGT
GCCGGGACGGCGCTGGTGGGCGATGGTCCTACGGTCGCTGCGCGAATCAACGAATATGCC
GCGCTTGGCATCGACAGTTTTGTGCTTTCGGGCTATCCGCATCTGGAAGAAGCGTATCGG
GTTGGCGAGTTGCTGTTCCCGCTTCTGGATGTCGCCATCCCGGAAATTCCCCAGCCGCAG
CCGCTGAATCCGCAAGGCGAAGCGGTGGCGAATGATTTTATCCCCCGTAAAGTCGCGCAA
AGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:381
Protein Molecular Weight:41736
Protein Theoretical pI:6
PDB File:1NQK
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Alkanesulfonate monooxygenase
MSLNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWL
VAASMIPVTQRLKFLVALRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDG
VFLDHSERYEASAEFTQVWRRLLQRETVDFNGKHIHVRGAKLLFPAIQQPYPPLYFGGSS
DVAQELAAEQVDLYLTWGEPPELVKEKIEQVRAKAAAHGRKIRFGIRLHVIVRETNDEAW
QAAERLISHLDDETIAKAQAAFARTDSVGQQRMAALHNGKRDNLEISPNLWAGVGLVRGG
AGTALVGDGPTVAARINEYAALGIDSFVLSGYPHLEEAYRVGELLFPLLDVAIPEIPQPQ
PLNPQGEAVANDFIPRKVAQS
References
External Links:
ResourceLink
Uniprot ID:P80645
Uniprot Name:SSUD_ECOLI
GenBank Gene ID:AJ237695
Genebank Protein ID:4583568
PDB ID:1NQK
Ecogene ID:EG13706
Ecocyc:EG13706
ColiBase:b0935
Kegg Gene:b0935
EchoBASE ID:EB3470
CCDB:SSUD_ECOLI
BacMap:16128902
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Eichhorn, E., Davey, C. A., Sargent, D. F., Leisinger, T., Richmond, T. J. (2002). "Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD." J Mol Biol 324:457-468. Pubmed: 12445781
  • Eichhorn, E., van der Ploeg, J. R., Leisinger, T. (1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli." J Biol Chem 274:26639-26646. Pubmed: 10480865
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "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." DNA Res 3:137-155. Pubmed: 8905232
  • Quadroni, M., Staudenmann, W., Kertesz, M., James, P. (1996). "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." Eur J Biochem 239:773-781. Pubmed: 8774726
  • van Der Ploeg, J. R., Iwanicka-Nowicka, R., Bykowski, T., Hryniewicz, M. M., Leisinger, T. (1999). "The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl." J Biol Chem 274:29358-29365. Pubmed: 10506196