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UniProtKB/Swiss-Prot entry P0A9S1


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

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Entry information
Entry name FUCO_ECOLI
Primary accession number P0A9S1
Secondary accession numbers P11549 Q2MA35
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on July 19, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 31)
Name and origin of the protein
Protein name Lactaldehyde reductase
Synonyms EC 1.1.1.77
Propanediol oxidoreductase
Gene name
Name: fucO
OrderedLocusNames: b2799, JW2770
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;
PubMed=2553671 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Y.M., Lu Z., Lin E.C.C.;
"Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol.";
J. Bacteriol. 171:6097-6105(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/17.12.4883; PubMed=2664711 [NCBI, ExPASy, EBI, Israel, Japan]
Lu Z., Lin E.C.C.;
"The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation.";
Nucleic Acids Res. 17:4883-4884(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2661535 [NCBI, ExPASy, EBI, Israel, Japan]
Conway T., Ingram L.O.;
"Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.";
J. Bacteriol. 171:3754-3759(1989).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-383.
STRAIN=K12;
PubMed=8385012 [NCBI, ExPASy, EBI, Israel, Japan]
Shao Z., Newman E.B.;
"Sequencing and characterization of the sdaB gene from Escherichia coli K-12.";
Eur. J. Biochem. 212:777-784(1993).
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
M31059; AAA23824.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15025; CAA33124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27177; AAA23825.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U29581; AAB40449.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75841.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07763; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR A32883; RDECLA.
RefSeq AP_003365.1; -.
NP_417279.1; -.
3D structure databases
PDB
1RRM; X-ray; 1.60 A; A/B=1-383.[ExPASy / RCSB / EBI]
2BI4; X-ray; 2.85 A; A/B=1-383.[ExPASy / RCSB / EBI]
2BL4; X-ray; 2.85 A; A/B=1-383.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1RRM; -.
2BI4; -.
2BL4; -.
ModBase P0A9S1.
Protein-protein interaction databases
IntAct P0A9S1; -.
Enzyme and pathway databases
BioCyc EcoCyc:LACTALDREDUCT-MON; -.
Organism-specific databases
EchoBASE EB0347; -.
EcoGene EG10351; fucO.
Ontologies
GO
GO:0008912; Molecular function: lactaldehyde reductase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR001670; Fe_AlcDHase.
IPR013460; Lactal_redase.
Graphical view of domain structure.
Pfam PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02638; lactal_redase; 1.
PROSITE PS00913; ADH_IRON_1; 1.
PS00060; ADH_IRON_2; 1.
BLOCKS P0A9S1.
Genome annotation databases
GeneID 947273; -.
GenomeReviews U00096_GR; b2799.
AP009048_GR; JW2770.
KEGG ecj:JW2770; -.
eco:b2799; -.
Phylogenomic databases
HOGENOM P0A9S1; -.
Genome annotation databases
CMR P0A9S1; b2799.
Other
ProtoNet P0A9S1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Complete proteome; Fucose metabolism; Iron; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   383  383     Lactaldehyde reductase. PRO_0000087824
CONFLICT   274   274        N -> T (in Ref. 2; CAA33124). 
STRAND   4     7  4      
STRAND   10    15  6      
HELIX   18    21  4      
HELIX   22    29  8      
STRAND   33    37  5      
HELIX   40    44  5      
HELIX   47    57  11      
STRAND   61    65  5      
HELIX   74    87  14      
STRAND   90    97  8      
HELIX   98   112  15      
HELIX   114   116  3      
HELIX   120   122  3      
STRAND   123   125  3      
STRAND   135   139  5      
STRAND   141   143  3      
TURN   146   148  3      
STRAND   150   156  7      
TURN   157   160  4      
STRAND   161   166  6      
HELIX   168   170  3      
STRAND   173   177  5      
HELIX   179   181  3      
TURN   182   184  3      
HELIX   187   206  20      
HELIX   212   233  22      
HELIX   237   257  21      
HELIX   261   273  13      
HELIX   277   292  16      
HELIX   293   295  3      
HELIX   299   306  8      
HELIX   316   333  18      
HELIX   340   343  4      
HELIX   347   349  3      
HELIX   350   358  9      
HELIX   361   365  5      
Sequence information
Length: 383 AA [This is the length of the unprocessed precursor] Molecular weight: 40645 Da [This is the MW of the unprocessed precursor] CRC64: F0103FED90CA33F3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMANRMILNE TAWFGRGAVG ALTDEVKRRG YQKALIVTDK TLVQCGVVAK VTDKMDAAGL 

        70         80         90        100        110        120 
AWAIYDGVVP NPTITVVKEG LGVFQNSGAD YLIAIGGGSP QDTCKAIGII SNNPEFADVR 

       130        140        150        160        170        180 
SLEGLSPTNK PSVPILAIPT TAGTAAEVTI NYVITDEEKR RKFVCVDPHD IPQVAFIDAD 

       190        200        210        220        230        240 
MMDGMPPALK AATGVDALTH AIEGYITRGA WALTDALHIK AIEIIAGALR GSVAGDKDAG 

       250        260        270        280        290        300 
EEMALGQYVA GMGFSNVGLG LVHGMAHPLG AFYNTPHGVA NAILLPHVMR YNADFTGEKY 

       310        320        330        340        350        360 
RDIARVMGVK VEGMSLEEAR NAAVEAVFAL NRDVGIPPHL RDVGVRKEDI PALAQAALDD 

       370        380 
VCTGGNPREA TLEDIVELYH TAW 

P0A9S1 in FASTA format

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