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UniProtKB/Swiss-Prot entry P00381


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

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Entry information
Entry name DYR_LACCA
Primary accession number P00381
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
Synonyms: dhfR
From
Lactobacillus casei [TaxID: 1582] 
Taxonomy Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(85)90174-X; PubMed=3928445 [NCBI, ExPASy, EBI, Israel, Japan]
Andrews J., Clore G.M., Davies R.W., Gronenborn A.M., Gronenborn B., Kalderon D., Papadopoulos P.C., Schaefer S., Sims P.F.G., Stancombe R.;
"Nucleotide sequence of the dihydrofolate reductase gene of methotrexate-resistant Lactobacillus casei.";
Gene 35:217-222(1985).
[2]
PROTEIN SEQUENCE OF 2-163.
PubMed=98527 [NCBI, ExPASy, EBI, Israel, Japan]
Freisheim J.H., Bitar K.G., Reddy A.V., Blankenship D.T.;
"Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei. Sequences of the cyanogen bromide peptides and complete sequences of the enzyme.";
J. Biol. Chem. 253:6437-6444(1978).
[3]
PROTEIN SEQUENCE OF 2-52.
DOI=10.1016/0006-291X(77)91482-6; PubMed=405008 [NCBI, ExPASy, EBI, Israel, Japan]
Batley K.E., Morris H.R.;
"Dihydrofolate reductase from Lactobacillus casei: N-terminal sequence and comparison with the substrate binding region of other reductases.";
Biochem. Biophys. Res. Commun. 75:1010-1014(1977).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=6815179 [NCBI, ExPASy, EBI, Israel, Japan]
Filman D.J., Bolin J.T., Matthews D.A., Kraut J.;
"Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7-A resolution. II. Environment of bound NADPH and implications for catalysis.";
J. Biol. Chem. 257:13663-13672(1982).
[5]
STRUCTURE BY NMR.
DOI=10.1021/bi00239a035; PubMed=1905571 [NCBI, ExPASy, EBI, Israel, Japan]
Carr M.D., Birdsall B., Frenkiel T.A., Bauer C.J., Jimenez-Barbero J., Polshakov V.I., McCormick J.E., Roberts G.C.K., Feeney J.;
"Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.";
Biochemistry 30:6330-6341(1991).
[6]
STRUCTURE BY NMR.
DOI=10.1021/bi00037a006; PubMed=7547901 [NCBI, ExPASy, EBI, Israel, Japan]
Morgan W.D., Birdsall B., Polshakov V.I., Sali D., Kompis I., Feeney J.;
"Solution structure of a brodimoprim analogue in its complex with Lactobacillus casei dihydrofolate reductase.";
Biochemistry 34:11690-11702(1995).
[7]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1997.1560; PubMed=9514736 [NCBI, ExPASy, EBI, Israel, Japan]
Gargaro A.R., Soteriou A., Frenkiel T.A., Bauer C.J., Birdsall B., Polshakov V.I., Barsukov I.L., Roberts G.C.K., Feeney J.;
"The solution structure of the complex of Lactobacillus casei dihydrofolate reductase with methotrexate.";
J. Mol. Biol. 277:119-134(1998).
[8]
STRUCTURE BY NMR.
PubMed=10091649 [NCBI, ExPASy, EBI, Israel, Japan]
Polshakov V.I., Birdsall B., Frenkiel T.A., Gargaro A.R., Feeney J.;
"Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate.";
Protein Sci. 8:467-481(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
M10922; AAA25237.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24036; RDLBD.
3D structure databases
PDB
1AO8; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
1BZF; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
1DIS; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
1DIU; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
1LUD; NMR; -; A=1-163.[ExPASy / RCSB / EBI]
2HM9; NMR; -; A=2-163.[ExPASy / RCSB / EBI]
2HQP; NMR; -; A=2-163.[ExPASy / RCSB / EBI]
3DFR; X-ray; 1.70 A; A=1-163.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AO8; -.
1BZF; -.
1DIS; -.
1DIU; -.
1LUD; -.
2HM9; -.
2HQP; -.
3DFR; -.
ModBase P00381.
Ontologies
GO
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).
GO:0046677; Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
GO:0031427; Biological process: response to methotrexate (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).
BLOCKS P00381.
ProtoNet P00381.
Other
LinkHub P00381; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antibiotic resistance; Direct protein sequencing; Methotrexate resistance; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   163  162     Dihydrofolate reductase. PRO_0000186393
DOMAIN   2   161  160     DHFR. 
NP_BIND   44    64  21     NADP (Potential). 
BINDING   27    27        Methotrexate. 
BINDING   32    32        Methotrexate. 
BINDING   58    58        Methotrexate. 
SITE   22    22  1     May be important for enzyme function. 
CONFLICT   9     9        D -> N (in Ref. 2; AA sequence). 
CONFLICT   91    91        P -> L (in Ref. 2; AA sequence). 
STRAND   3     8  6      
STRAND   13    16  4      
HELIX   25    33  9      
TURN   34    37  4      
STRAND   38    43  6      
HELIX   44    49  6      
STRAND   50    54  5      
STRAND   58    63  6      
STRAND   74    79  6      
HELIX   80    89  10      
STRAND   95    97  3      
HELIX   101   106  6      
HELIX   108   110  3      
STRAND   113   121  9      
STRAND   126   128  3      
HELIX   134   136  3      
STRAND   137   145  9      
HELIX   150   152  3      
STRAND   154   161  8      
Sequence information
Length: 163 AA [This is the length of the unprocessed precursor] Molecular weight: 18439 Da [This is the MW of the unprocessed precursor] CRC64: 1E4B556ED7A750D1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAFLWAQDR DGLIGKDGHL PWHLPDDLHY FRAQTVGKIM VVGRRTYESF PKRPLPERTN 

        70         80         90        100        110        120 
VVLTHQEDYQ AQGAVVVHDV AAVFAYAKQH PDQELVIAGG AQIFTAFKDD VDTLLVTRLA 

       130        140        150        160 
GSFEGDTKMI PLNWDDFTKV SSRTVEDTNP ALTHTYEVWQ KKA 

P00381 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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