GEOSE:A0A087LEM1

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	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	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
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References

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