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ECOLI:DYR

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) folA (synonyms: tmrA)
Protein Name(s) Dihydrofolate reductase
External Links
UniProt P0ABQ4
EMBL J01609
X05108
U00096
AP009048
PIR A93704
RefSeq NP_414590.1
YP_488354.1
PDB 1DDR
1DDS
1DHI
1DHJ
1DRA
1DRB
1DRE
1DRH
1DYH
1DYI
1DYJ
1JOL
1JOM
1RA1
1RA2
1RA3
1RA8
1RA9
1RB2
1RB3
1RC4
1RD7
1RE7
1RF7
1RG7
1RH3
1RX1
1RX2
1RX3
1RX4
1RX5
1RX6
1RX7
1RX8
1RX9
1TDR
2ANO
2ANQ
2D0K
2DRC
2INQ
3DAU
3DRC
3K74
3KFY
3OCH
3QL3
3QYL
3QYO
3R33
4DFR
4EIG
4EIZ
4EJ1
4FHB
4GH8
4I13
4I1N
4KJJ
4KJK
4KJL
4NX6
4NX7
5DFR
6DFR
7DFR
PDBsum 1DDR
1DDS
1DHI
1DHJ
1DRA
1DRB
1DRE
1DRH
1DYH
1DYI
1DYJ
1JOL
1JOM
1RA1
1RA2
1RA3
1RA8
1RA9
1RB2
1RB3
1RC4
1RD7
1RE7
1RF7
1RG7
1RH3
1RX1
1RX2
1RX3
1RX4
1RX5
1RX6
1RX7
1RX8
1RX9
1TDR
2ANO
2ANQ
2D0K
2DRC
2INQ
3DAU
3DRC
3K74
3KFY
3OCH
3QL3
3QYL
3QYO
3R33
4DFR
4EIG
4EIZ
4EJ1
4FHB
4GH8
4I13
4I1N
4KJJ
4KJK
4KJL
4NX6
4NX7
5DFR
6DFR
7DFR
DisProt DP00301
ProteinModelPortal P0ABQ4
SMR P0ABQ4
DIP DIP-35824N
IntAct P0ABQ4
MINT MINT-1239602
STRING 511145.b0048
BindingDB P0ABQ4
ChEMBL CHEMBL2364669
SWISS-2DPAGE P0ABQ4
PaxDb P0ABQ4
PRIDE P0ABQ4
EnsemblBacteria AAC73159
BAB96616
GeneID 12933205
944790
KEGG ecj:Y75_p0048
eco:b0048
PATRIC 32115195
EchoBASE EB0322
EcoGene EG10326
eggNOG COG0262
HOGENOM HOG000040233
InParanoid P0ABQ4
KO K00287
OMA TSYAFVH
OrthoDB EOG6KT2V2
PhylomeDB P0ABQ4
BioCyc EcoCyc:DIHYDROFOLATEREDUCT-MONOMER
ECOL316407:JW0047-MONOMER
MetaCyc:DIHYDROFOLATEREDUCT-MONOMER
SABIO-RK P0ABQ4
UniPathway UPA00077
EvolutionaryTrace P0ABQ4
PRO PR:P0ABQ4
Proteomes UP000000318
UP000000625
Genevestigator P0ABQ4
GO GO:0004146
GO:0050661
GO:0009257
GO:0046656
GO:0006545
GO:0009165
GO:0006730
GO:0046677
GO:0042493
GO:0031427
Gene3D 3.40.430.10
InterPro IPR012259
IPR024072
IPR017925
IPR001796
Pfam PF00186
PIRSF PIRSF000194
PRINTS PR00070
SUPFAM SSF53597
PROSITE PS00075
PS51330

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004146

dihydrofolate reductase activity

PMID:26147643[1]

ECO:0000315

F

Typically, dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). DHFR acts in a catalytic cycle of 5 different intermediates. In the mutant (by changing Leu 28 to Phe), the dissociation rate of the enzyme:substrate complex increases by 10-20 fold. In addition, the rates of the exchange of the excited closed states are very different in the mutants, despite the similarities found in the ground states of the mutant and wild-types. There are 2 pathways, intrinsic and allosteric pathways that this enzyme can take depending on the environmental conditions.

complete
CACAO 11420

enables

GO:0070402

NADPH binding

PMID:9012674[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051870

methotrexate binding

PMID:9012674[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005542

folic acid binding

PMID:9012674[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070401

NADP+ binding

PMID:9012674[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005542

folic acid binding

PMID:14717591[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070401

NADP+ binding

PMID:14717591[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051871

dihydrofolic acid binding

PMID:14717591[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070402

NADPH binding

PMID:14717591[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500

F

Seeded From UniProt

complete

involved_in

GO:0046655

folic acid metabolic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
ZFIN:ZDB-GENE-010406-5

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
UniProtKB:P00374
UniProtKB:P9WNX1

P

Seeded From UniProt

complete

involved_in

GO:0046452

dihydrofolate metabolic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
UniProtKB:P00374

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10326
PANTHER:PTN000167378

C

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10326
FB:FBgn0004087
MGI:MGI:94890
PANTHER:PTN000167322
PomBase:SPCC1223.08c
RGD:2500
UniProtKB:P00374
UniProtKB:P9WNX1
UniProtKB:Q86XF0
dictyBase:DDB_G0286755

F

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:6444603[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

PMID:46[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796
InterPro:IPR012259
InterPro:IPR017925

F

Seeded From UniProt

complete

involved_in

GO:0006545

glycine biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012259

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796
InterPro:IPR012259

P

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012259

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796
InterPro:IPR012259
InterPro:IPR017925

P

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.5.1.3

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0006730

one-carbon metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0554

P

Seeded From UniProt

complete

involved_in

GO:0031427

response to methotrexate

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0487

P

Seeded From UniProt

complete

involved_in

GO:0046677

response to antibiotic

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0817
UniProtKB-KW:KW-0046

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00077

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Oyen, D et al. (2015) Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway. J. Am. Chem. Soc. 137 9459-68 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Sawaya, MR & Kraut, J (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 586-603 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Schnell, JR et al. (2004) Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. Biochemistry 43 374-83 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. Rood, JI et al. (1980) Cloning of the Escherichia coli K-12 dihydrofolate reductase gene following mu-mediated transposition. Gene 8 255-65 PubMed GONUTS page
  6. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  7. Baccanari, D et al. (1975) Purification and properties of Escherichia coli dihydrofolate reductase. Biochemistry 14 5267-73 PubMed GONUTS page