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GEOSE:A0A087LEM1

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Species (Taxon ID) Geobacillus stearothermophilus (Bacillus stearothermophilus). (1422)
Gene Name(s) No Information Provided.
Protein Name(s) Dihydrofolate reductase (ECO:0000256 with PIRNR:PIRNR000194)
External Links
UniProt A0A087LEM1
EMBL JPYV01000160
LDNS01000002
RefSeq WP_033010007.1
EnsemblBacteria KFL16074
KFX32045
UniPathway UPA00077
Proteomes UP000029337
UP000037609
GO GO:0004146
GO:0050661
GO:0006545
GO:0009165
GO:0006730
GO:0046654
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:16114879[1]

ECO:0000314

F

The three-dimensional structure of the dihydrofoate reductase (via X-ray crystallography) in Bacillus Stearothermophilus is iterated by Figure 3. This structure of Bacillus Stearothermophilus DHFR is the first monomeric DHFR structure from a thermophilic organism; there is also comparison between E. coli and T. maritima enzymes. IDA was used because this was the actual determination of the structure; the comparison to the other 2 enzymes helps support the functional conservation.

complete
CACAO 11999

GO:0004146

dihydrofolate reductase activity

PMID:16114879[1]

ECO:0000315

F

Figure 4 shows BsDHFR activity as a function of reaction conditions through its pH dependence within MTEN buffer at different pH values and 40 °C with the rest at standard conditions. Optimum temperature for neutral pH of 7 was 75*C although enzyme stability was seen at pH 6.8 as a function of temperature due to very rapid loss of activity in the absence of substrate above 64 °C. pKa under standard assay was 7.5. The formation of THF is shown to be sensitive to pH since as pH increases, activity declines.

complete
CACAO 12000

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

enables

GO:0016491

oxidoreductase activity

GO_REF:0000038

ECO:0000323

imported automatically 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:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0554

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0560

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. 1.0 1.1 Kim, HS et al. (2005) Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues. Biochemistry 44 11428-39 PubMed GONUTS page