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UniProtKB/Swiss-Prot entry P80644


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SSUE_ECOLI
Primary accession number P80644
Secondary accession number P75854
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 60)
Name and origin of the protein
Protein name FMN reductase
Synonyms EC 1.5.1.29
Sulfate starvation-induced protein 4
SSI4
Gene name
Name: ssuE
Synonyms: ycbP
OrderedLocusNames: b0937, JW0920
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1074/jbc.274.41.29358; PubMed=10506196 [NCBI, ExPASy, EBI, Israel, Japan]
Van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M.M., Leisinger T.;
"The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl.";
J. Biol. Chem. 274:29358-29365(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-14.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8774726 [NCBI, ExPASy, EBI, Israel, Japan]
Quadroni M., Staudenmann W., Kertesz M.A., James P.;
"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.";
Eur. J. Biochem. 239:773-781(1996).
[6]
CHARACTERIZATION.
DOI=10.1074/jbc.274.38.26639; PubMed=10480865 [NCBI, ExPASy, EBI, Israel, Japan]
Eichhorn E., van der Ploeg J.R., Leisinger T.;
"Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli.";
J. Biol. Chem. 274:26639-26646(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ237695; CAB40389.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74023.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35692.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64833; H64833.
RefSeq AP_001567.1; -.
NP_415457.1; -.
3D structure databases
ModBase P80644.
Protein-protein interaction databases
DIP DIP:10929N; -.
IntAct P80644; -.
Enzyme and pathway databases
BioCyc EcoCyc:MON0-146; -.
MetaCyc:MON0-146; -.
Organism-specific databases
EchoBASE EB3472; -.
EcoGene EG13708; ssuE.
Family and domain databases
InterPro IPR005025; FMN_red.
Graphical view of domain structure.
Pfam PF03358; FMN_red; 1.
Pfam graphical view of domain structure.
BLOCKS P80644.
Genome annotation databases
GeneID 945947; -.
GenomeReviews U00096_GR; b0937.
AP009048_GR; JW0920.
KEGG ecj:JW0920; -.
eco:b0937; -.
Phylogenomic databases
HOGENOM P80644; -.
Genome annotation databases
CMR P80644; b0937.
Other
ProtoNet P80644.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; FMN; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   191  191     FMN reductase. PRO_0000160591
Sequence information
Length: 191 AA [This is the length of the unprocessed precursor] Molecular weight: 21253 Da [This is the MW of the unprocessed precursor] CRC64: 2371808C97CEE532 [This is a checksum on the sequence]
        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 

P80644 in FASTA format

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