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Protein

Dihydroneopterin triphosphate 2'-epimerase

Gene

folX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP) (PubMed:9182560) (PubMed:9651328). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli (PubMed:19897652).3 Publications

Catalytic activityi

7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate.2 Publications

Kineticsi

  1. KM=13 µM for 7,8-dihydroneopterin triphosphate1 Publication
  2. KM=149 µM for 7,8-dihydroneopterin1 Publication
  3. KM=66 µM for 7,8-dihydromonapterin1 Publication
  1. Vmax=480 µmol/h/mg enzyme for the epimerization of 7,8-dihydroneopterin triphosphate1 Publication
  2. Vmax=0.95 µmol/h/mg enzyme for the epimerization of 7,8-dihydroneopterin1 Publication
  3. Vmax=0.67 µmol/h/mg enzyme for the epimerization of 7,8-dihydromonapterin1 Publication

GO - Molecular functioni

GO - Biological processi

  • folic acid-containing compound metabolic process Source: EcoCyc

Keywordsi

Molecular functionIsomerase

Enzyme and pathway databases

BioCyciEcoCyc:H2NTPEPIM-MONOMER
MetaCyc:H2NTPEPIM-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroneopterin triphosphate 2'-epimerase1 Publication (EC:5.1.99.-2 Publications)
Alternative name(s):
D-erythro-7,8-dihydroneopterin triphosphate epimerase
Gene namesi
Name:folX
Ordered Locus Names:b2303, JW2300
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14263 folX

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show no detectable growth defect on complete and minimal medium (PubMed:9651328). The folX deletion selectively eliminates monapterin production and secretion, but has no effect on the intra- and extracellular folate profiles (PubMed:19897652).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001682952 – 120Dihydroneopterin triphosphate 2'-epimeraseAdd BLAST119

Proteomic databases

EPDiP0AC19
PaxDbiP0AC19
PRIDEiP0AC19

Interactioni

Subunit structurei

Homooctamer.2 Publications

Protein-protein interaction databases

BioGridi4260518, 7 interactors
DIPiDIP-9679N
IntActiP0AC19, 3 interactors
STRINGi316385.ECDH10B_2465

Structurei

Secondary structure

1120
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 19Combined sources15
Helixi23 – 27Combined sources5
Beta strandi30 – 41Combined sources12
Helixi42 – 46Combined sources5
Helixi47 – 49Combined sources3
Helixi57 – 69Combined sources13
Beta strandi71 – 74Combined sources4
Helixi76 – 87Combined sources12
Beta strandi94 – 103Combined sources10
Beta strandi109 – 119Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B9LX-ray2.90A/B/C/D/E/F/G/H1-120[»]
ProteinModelPortaliP0AC19
SMRiP0AC19
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC19

Family & Domainsi

Sequence similaritiesi

Belongs to the DHNA family.Curated

Phylogenomic databases

eggNOGiENOG4105KKP Bacteria
COG1539 LUCA
HOGENOMiHOG000217626
InParanoidiP0AC19
KOiK07589
OMAiTILYAAQ
PhylomeDBiP0AC19

Family and domain databases

CDDicd00534 DHNA_DHNTPE, 1 hit
InterProiView protein in InterPro
IPR006157 FolB_dom
PfamiView protein in Pfam
PF02152 FolB, 1 hit
SMARTiView protein in SMART
SM00905 FolB, 1 hit
TIGRFAMsiTIGR00526 folB_dom, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED
60 70 80 90 100
INDALNYRTV TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI
110 120
DKLHALRYAD SVSMTLSWQR
Length:120
Mass (Da):14,082
Last modified:January 23, 2007 - v2
Checksum:i5DDFF76540827ED6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27 – 30NNRQ → KQPS in AAB47972 (PubMed:9182560).Curated4
Sequence conflicti48 – 49SE → RQ in AAB47972 (PubMed:9182560).Curated2
Sequence conflicti55L → M in AAB47972 (PubMed:9182560).Curated1
Sequence conflicti107R → A in AAB47972 (PubMed:9182560).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96709 Genomic DNA Translation: CAA65471.1
U47639 Genomic DNA Translation: AAB47972.1
AP009048 Genomic DNA Translation: BAA16140.1
U00096 Genomic DNA Translation: AAC75363.1
PIRiE65002
RefSeqiNP_416806.1, NC_000913.3
WP_000068457.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75363; AAC75363; b2303
BAA16140; BAA16140; BAA16140
GeneIDi946781
KEGGiecj:JW2300
eco:b2303
PATRICifig|1411691.4.peg.4431

Similar proteinsi

Entry informationi

Entry nameiFOLX_ECOLI
AccessioniPrimary (citable) accession number: P0AC19
Secondary accession number(s): P77796, P80449
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 98 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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