Reviewed, UniProtKB/Swiss-Prot P80645 (SSUD_ECOLI)

Names and origin

Protein names

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 names

Name:	ssuD
Synonyms:	ycbN
Ordered Locus Names:	b0935, JW0918

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. HAMAP MF_01229
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.

Ontologies

Keywords
Ligand	FMN
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	alkanesulfonate catabolic process Ref.1 Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alkanesulfonate monooxygenase activity Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 381

380

Alkanesulfonate monooxygenase HAMAP MF_01229

PRO_0000216706

Natural variations

Natural variant

298

1

R → C in strain: K12 / MC4100; inactive.

Experimental info

Mutagenesis

298

1

R → C: Loss of activity. Ref.6

Sequence conflict

19

1

G → Q AA sequence Ref.5

Secondary structure

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381

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

14 – 17

4

Helix

29 – 42

14

Beta strand

45 – 49

5

Helix

58 – 63

6

Beta strand

73 – 78

6

Turn

80 – 82

3

Helix

85 – 98

14

Beta strand

103 – 107

5

Helix

113 – 119

7

Helix

127 – 142

16

Turn

143 – 145

3

Beta strand

148 – 151

4

Beta strand

156 – 160

5

Beta strand

167 – 172

6

Beta strand

174 – 177

4

Helix

181 – 190

10

Beta strand

192 – 197

6

Helix

201 – 216

16

Turn

217 – 219

3

Beta strand

223 – 235

13

Helix

236 – 246

11

Turn

247 – 249

3

Helix

252 – 261

10

Beta strand

285 – 287

3

Helix

292 – 295

4

Beta strand

296 – 300

5

Beta strand

304 – 308

5

Helix

309 – 320

12

Turn

321 – 323

3

Beta strand

324 – 330

7

Helix

334 – 344

11

Helix

346 – 348

3

Sequences

	Sequence		Length	Mass (Da)
	P80645-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4D05E510487999C6	FASTA	381	41,736
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

F64833.

RefSeq

AP_001565.1.
NP_415455.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M41	X-ray	2.30	A/B	2-381	[»]
1NQK	X-ray	2.20	A	1-381	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10928N.

STRING

P80645.

Genome annotation databases

GeneID

945557.

GenomeReviews

Gene locus JW0918 in contig AP009048_GR.
Gene locus b0935 in contig U00096_GR.

KEGG

ecj:JW0918.
eco:b0935.

Organism-specific databases

EchoBASE

EB3470.

EcoGene

EG13706. ssuD.

CMR

Search...

Phylogenomic databases

eggNOG

COG2141.

HOGENOM

HBG639644.

OMA

NIFWFLP.

Enzyme and pathway databases

BioCyc

EcoCyc:MONOMER-162.
ECOL168927:B0935-MONOMER.
MetaCyc:MONOMER-162.

Gene expression databases

Genevestigator

P80645.

Family and domain databases

HAMAP

MF_01229. Alkanesulf_monooxygen.
[Tree]

InterPro

IPR019911. Alkanesulphonate_mOase_FMN-dep.
IPR011251. Luciferase-like.
[Graphical view]

TIGRFAMs

TIGR03565. Alk_sulf_monoox. 1 hit.

ProtoNet

Search...

Entry information

Entry name

SSUD_ECOLI

Accession

Primary (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:	February 9, 2010
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)