Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13706. ssuD.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi298 – 2981R → C: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 381380Alkanesulfonate monooxygenasePRO_0000216706Add
BLAST

Proteomic databases

PaxDbiP80645.

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 interactions.
DIPiDIP-10928N.
IntActiP80645. 10 interactions.
STRINGi511145.b0935.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi14 – 174Combined sources
Helixi29 – 4214Combined sources
Beta strandi45 – 495Combined sources
Helixi58 – 636Combined sources
Beta strandi73 – 786Combined sources
Turni80 – 823Combined sources
Helixi85 – 9814Combined sources
Beta strandi103 – 1075Combined sources
Helixi113 – 1197Combined sources
Helixi127 – 14216Combined sources
Turni143 – 1453Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi167 – 1726Combined sources
Beta strandi174 – 1774Combined sources
Helixi181 – 19010Combined sources
Beta strandi192 – 1976Combined sources
Helixi201 – 21616Combined sources
Turni217 – 2193Combined sources
Beta strandi223 – 23513Combined sources
Helixi236 – 24611Combined sources
Turni247 – 2493Combined sources
Helixi252 – 26110Combined sources
Beta strandi285 – 2873Combined sources
Helixi292 – 2954Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi304 – 3085Combined sources
Helixi309 – 32012Combined sources
Turni321 – 3233Combined sources
Beta strandi324 – 3307Combined sources
Helixi334 – 34411Combined sources
Helixi346 – 3483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M41X-ray2.30A/B2-381[»]
1NQKX-ray2.20A1-381[»]
ProteinModelPortaliP80645.
SMRiP80645. Positions 1-362.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → Q AA sequence (PubMed:8774726).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981R → C in strain: K12 / MC4100; inactive.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1M41X-ray2.30A/B2-381[»]
1NQKX-ray2.20A1-381[»]
ProteinModelPortaliP80645.
SMRiP80645. Positions 1-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP80645.

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: September 7, 2016
This is version 138 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.