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Protein

Alkanesulfonate monooxygenase

Gene

ssuD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

GO - Molecular functioni

  • alkanesulfonate monooxygenase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • alkanesulfonate catabolic process Source: EcoCyc
  • response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER-162.
ECOL316407:JW0918-MONOMER.
MetaCyc:MONOMER-162.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ssuD
Synonyms:ycbN
Ordered Locus Names:b0935, JW0918
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13706. ssuD.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi298R → C: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002167062 – 381Alkanesulfonate monooxygenaseAdd BLAST380

Proteomic databases

PaxDbiP80645.
PRIDEiP80645.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ssuEP806442EBI-561637,EBI-1121047

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260022. 10 interactors.
DIPiDIP-10928N.
IntActiP80645. 10 interactors.
STRINGi511145.b0935.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Beta strandi14 – 17Combined sources4
Helixi29 – 42Combined sources14
Beta strandi45 – 49Combined sources5
Helixi58 – 63Combined sources6
Beta strandi73 – 78Combined sources6
Turni80 – 82Combined sources3
Helixi85 – 98Combined sources14
Beta strandi103 – 107Combined sources5
Helixi113 – 119Combined sources7
Helixi127 – 142Combined sources16
Turni143 – 145Combined sources3
Beta strandi148 – 151Combined sources4
Beta strandi156 – 160Combined sources5
Beta strandi167 – 172Combined sources6
Beta strandi174 – 177Combined sources4
Helixi181 – 190Combined sources10
Beta strandi192 – 197Combined sources6
Helixi201 – 216Combined sources16
Turni217 – 219Combined sources3
Beta strandi223 – 235Combined sources13
Helixi236 – 246Combined sources11
Turni247 – 249Combined sources3
Helixi252 – 261Combined sources10
Beta strandi285 – 287Combined sources3
Helixi292 – 295Combined sources4
Beta strandi296 – 300Combined sources5
Beta strandi304 – 308Combined sources5
Helixi309 – 320Combined sources12
Turni321 – 323Combined sources3
Beta strandi324 – 330Combined sources7
Helixi334 – 344Combined sources11
Helixi346 – 348Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M41X-ray2.30A/B2-381[»]
1NQKX-ray2.20A1-381[»]
ProteinModelPortaliP80645.
SMRiP80645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80645.

Family & Domainsi

Sequence similaritiesi

Belongs to the SsuD family.Curated

Phylogenomic databases

eggNOGiENOG4105D4R. Bacteria.
COG2141. LUCA.
HOGENOMiHOG000134568.
InParanoidiP80645.
KOiK04091.
OMAiDYDGKHI.
PhylomeDBiP80645.

Family and domain databases

Gene3Di3.20.20.30. 2 hits.
HAMAPiMF_01229. Alkanesulf_monooxygen. 1 hit.
InterProiIPR019911. Alkanesulphonate_mOase_FMN-dep.
IPR011251. Luciferase-like_dom.
[Graphical view]
PfamiPF00296. Bac_luciferase. 1 hit.
[Graphical view]
SUPFAMiSSF51679. SSF51679. 1 hit.
TIGRFAMsiTIGR03565. alk_sulf_monoox. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP
60 70 80 90 100
TGRSCEDAWL VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN
110 120 130 140 150
GRALFNLVTG SDPQELAGDG VFLDHSERYE ASAEFTQVWR RLLQRETVDF
160 170 180 190 200
NGKHIHVRGA KLLFPAIQQP YPPLYFGGSS DVAQELAAEQ VDLYLTWGEP
210 220 230 240 250
PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW QAAERLISHL
260 270 280 290 300
DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
310 320 330 340 350
AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPLLD
360 370 380
VAIPEIPQPQ PLNPQGEAVA NDFIPRKVAQ S
Length:381
Mass (Da):41,736
Last modified:January 23, 2007 - v3
Checksum:i4D05E510487999C6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19G → Q AA sequence (PubMed:8774726).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti298R → C in strain: K12 / MC4100; inactive. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237695 Genomic DNA. Translation: CAB40391.1.
U00096 Genomic DNA. Translation: AAC74021.1.
AP009048 Genomic DNA. Translation: BAA35690.1.
PIRiF64833.
RefSeqiNP_415455.1. NC_000913.3.
WP_000056006.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74021; AAC74021; b0935.
BAA35690; BAA35690; BAA35690.
GeneIDi945557.
KEGGiecj:JW0918.
eco:b0935.
PATRICi32117089. VBIEscCol129921_0969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237695 Genomic DNA. Translation: CAB40391.1.
U00096 Genomic DNA. Translation: AAC74021.1.
AP009048 Genomic DNA. Translation: BAA35690.1.
PIRiF64833.
RefSeqiNP_415455.1. NC_000913.3.
WP_000056006.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M41X-ray2.30A/B2-381[»]
1NQKX-ray2.20A1-381[»]
ProteinModelPortaliP80645.
SMRiP80645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260022. 10 interactors.
DIPiDIP-10928N.
IntActiP80645. 10 interactors.
STRINGi511145.b0935.

Proteomic databases

PaxDbiP80645.
PRIDEiP80645.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74021; AAC74021; b0935.
BAA35690; BAA35690; BAA35690.
GeneIDi945557.
KEGGiecj:JW0918.
eco:b0935.
PATRICi32117089. VBIEscCol129921_0969.

Organism-specific databases

EchoBASEiEB3470.
EcoGeneiEG13706. ssuD.

Phylogenomic databases

eggNOGiENOG4105D4R. Bacteria.
COG2141. LUCA.
HOGENOMiHOG000134568.
InParanoidiP80645.
KOiK04091.
OMAiDYDGKHI.
PhylomeDBiP80645.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER-162.
ECOL316407:JW0918-MONOMER.
MetaCyc:MONOMER-162.

Miscellaneous databases

EvolutionaryTraceiP80645.
PROiP80645.

Family and domain databases

Gene3Di3.20.20.30. 2 hits.
HAMAPiMF_01229. Alkanesulf_monooxygen. 1 hit.
InterProiIPR019911. Alkanesulphonate_mOase_FMN-dep.
IPR011251. Luciferase-like_dom.
[Graphical view]
PfamiPF00296. Bac_luciferase. 1 hit.
[Graphical view]
SUPFAMiSSF51679. SSF51679. 1 hit.
TIGRFAMsiTIGR03565. alk_sulf_monoox. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSSUD_ECOLI
AccessioniPrimary (citable) accession number: P80645
Secondary accession number(s): P75852, Q9RM46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.