P80644 (SSUE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FMN reductase (NADPH)
EC=1.5.1.38

Alternative name(s):
FMN reductase
Sulfate starvation-induced protein 4
Short name=SSI4

Gene names

Name:	ssuE
Synonyms:	ycbP
Ordered Locus Names:	b0937, JW0920

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
Catalytic activity	FMNH2 + NADP+ = FMN + NADPH.
Subunit structure	Homodimer.
Induction	Repressed by sulfate or cysteine.
Sequence similarities	Belongs to the ssuE family.

Ontologies

Keywords
Ligand	FMN NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	alkanesulfonate catabolic process Inferred from mutant phenotype Ref.1. Source: EcoCyc cellular response to sulfate starvation Inferred from expression pattern Ref.5. Source: EcoCyc
Molecular function	FMN reductase activity Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 191	191	FMN reductase (NADPH)		PRO_0000160591

Sequences

	Sequence		Length	Mass (Da)
	P80644 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 2371808C97CEE532	FASTA	191	21,253
	10 20 30 40 50 60 MRVITLAGSP RFPSRSSSLL EYAREKLNGL DVEVYHWNLQ NFAPEDLLYA RFDSPALKTF 70 80 90 100 110 120 TEQLQQADGL IVATPVYKAA YSGALKTLLD LLPERALQGK VVLPLATGGT VAHLLAVDYA 130 140 150 160 170 180 LKPVLSALKA QEILHGVFAD DSQVIDYHHR PQFTPNLQTR LDTALETFWQ ALHRRDVQVP 190 DLLSLRGNAH A

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 1-14. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ237695 Genomic DNA. Translation: CAB40389.1. U00096 Genomic DNA. Translation: AAC74023.1. AP009048 Genomic DNA. Translation: BAA35692.1.
PIR	H64833.
RefSeq	NP_415457.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P80644.
SMR	P80644. Positions 2-176.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10929N.
IntAct	P80644. 3 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004628; EBESCP00000004628; EBESCG00000003773. EBESCT00000015755; EBESCP00000015046; EBESCG00000014815.
GeneID	945947.
GenomeReviews	Gene locus JW0920 in contig AP009048_GR. Gene locus b0937 in contig U00096_GR.
KEGG	ecj:JW0920. eco:b0937.
PATRIC	32117093. VBIEscCol129921_0971.
Organism-specific databases
EchoBASE	EB3472.
EcoGene	EG13708. ssuE.
Phylogenomic databases
eggNOG	COG0431.
GeneTree	EBGT00050000010184.
HOGENOM	HBG697130.
OMA	ARFDSPQ.
PhylomeDB	P80644.
ProtClustDB	PRK10569.
Enzyme and pathway databases
BioCyc	EcoCyc:MONOMER0-146. MetaCyc:MONOMER0-146.
Gene expression databases
Genevestigator	P80644.
Family and domain databases
InterPro	IPR005025. FMN_red. IPR020048. NADPH-dep_FMN_reduc_SsuE. [Graphical view]
KO	K00299.
Pfam	PF03358. FMN_red. 1 hit. [Graphical view]
TIGRFAMs	TIGR03567. FMN_reduc_SsuE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SSUE_ECOLI

Accession

Primary (citable) accession number: P80644
Secondary accession number(s): P75854

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program