Reviewed, UniProtKB/Swiss-Prot A7ZYN8 (SSUD_ECOHS)

Names and origin

Protein names

Recommended name:
    Alkanesulfonate monooxygenase
    EC=1.14.14.5
Alternative name(s):
    FMNH2-dependent aliphatic sulfonate monooxygenase

Gene names

Name:	ssuD
Ordered Locus Names:	EcHS_A1044

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the desulfonation of aliphatic sulfonates By similarity.
Catalytic activity	An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) + O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O.
Subunit structure	Homotetramer By similarity.
Miscellaneous	FMNH(2) which is absolutely required for this enzymatic reaction, is provided by ssuE By similarity.
Sequence similarities	Belongs to the ssuD family.

Ontologies

Keywords
Ligand	FMN
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alkanesulfonate monooxygenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	Alkanesulfonate monooxygenase		PRO_1000066820

Sequences

	Sequence		Length	Mass (Da)
	A7ZYN8-1 [UniParc]. Last modified October 23, 2007. Version 1. 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

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV05392.1.
RefSeq	YP_001457775.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5591079.
GenomeReviews	Gene locus EcHS_A1044 in contig CP000802_GR.
KEGG	ecx:EcHS_A1044.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01229. [Tree]
InterPro	IPR011251. Luciferase-like_bac. IPR016048. Luciferase_mOase. [Graphical view]
Gene3D	G3DSA:3.20.20.30. Luciferase_like. 1 hit.
Pfam	PF00296. Bac_luciferase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSUD_ECOHS

Accession

Primary (citable) accession number: A7ZYN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	November 25, 2008
This is version 10 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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