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ECOLI:FOLX

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Contents

Species (Taxon ID) Escherichia coli (strain K12). ([1])
Gene Name(s) folX
Protein Name(s) D-erythro-7,8-dihydroneopterin triphosphate epimerase

Dihydroneopterin triphosphate 2'-epimerase

External Links
EMBL X96709
U47639
AP009048
U00096
PIR E65002
RefSeq NP_416806.1
PDB 1B9L
PDBsum 1B9L
ProteinModelPortal P0AC19
SMR P0AC19
IntAct P0AC19
EnsemblBacteria EBESCT00000000981
EBESCT00000018003
GeneID 946781
GenomeReviews AP009048_GR
U00096_GR
KEGG ecj:JW2300
eco:b2303
EchoBASE EB4011
EcoGene EG14263
eggNOG COG1539
GeneTree EBGT00050000009852
HOGENOM HBG635896
OMA RTYIGIK
ProtClustDB PRK11245
BioCyc EcoCyc:H2NTPEPIM-MONOMER
MetaCyc:H2NTPEPIM-MONOMER
Genevestigator P0AC19
GO GO:0004150
GO:0008719
GO:0006760
InterPro IPR006157
Pfam PF02152
SMART SM00905
TIGRFAMs TIGR00526

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004150

dihydroneopterin aldolase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006157

F

Seeded From UniProt

GO:0006760

folic acid-containing compound metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006157

P

Seeded From UniProt

GO:0006760

folic acid-containing compound metabolic process

PMID:19897652[1]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0008719

dihydroneopterin triphosphate 2'-epimerase activity

PMID:9651328[2]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

GO:0016853

isomerase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0413

F

Seeded From UniProt


Notes

References

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

  1. Pribat A et al. (2010) FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa. J Bacteriol 192: 475-82 PubMed GONUTS page
  2. Haussmann C et al. (1998) Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J Biol Chem 273: 17418-24 PubMed GONUTS page
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