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UniProtKB/Swiss-Prot entry P0ABQ5

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

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Entry information
Entry name DYR_ECOL6
Primary accession number P0ABQ5
Secondary accession number P00379
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 26)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
OrderedLocusNames: c0058
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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
AE014075; AAN78554.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_752010.1; -.
3D structure databases
SMR P0ABQ5; 1-159.
DisProt DP00301; -.
ModBase P0ABQ5.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165; Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
Pfam PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1035973; -.
GenomeReviews AE014075_GR; c0058.
KEGG ecc:c0058; -.
Phylogenomic databases
HOGENOM P0ABQ5; -.
Other
BindingDB P0ABQ5; -.
Genome annotation databases
CMR P0ABQ5; c0058.
Other
ProtoNet P0ABQ5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   159  159     Dihydrofolate reductase. PRO_0000186388
DOMAIN   1   158  158     DHFR. 
Sequence information
Length: 159 AA [This is the length of the unprocessed precursor] Molecular weight: 17999 Da [This is the MW of the unprocessed precursor] CRC64: 6A03CDCD7F5F8562 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI 

        70         80         90        100        110        120 
ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE 

       130        140        150 
GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR
P0ABQ5 in FASTA format

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