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Protein

Dihydroneopterin triphosphate 2'-epimerase

Gene

folX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciEcoCyc:H2NTPEPIM-MONOMER.
ECOL316407:JW2300-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14263. folX.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 120119Dihydroneopterin triphosphate 2'-epimerasePRO_0000168295Add
BLAST

Proteomic databases

EPDiP0AC19.
PaxDbiP0AC19.
PRIDEiP0AC19.

Interactioni

Subunit structurei

Homooctamer.2 Publications

Protein-protein interaction databases

BioGridi4260518. 7 interactions.
DIPiDIP-9679N.
IntActiP0AC19. 3 interactions.
STRINGi511145.b2303.

Structurei

Secondary structure

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1915Combined sources
Helixi23 – 275Combined sources
Beta strandi30 – 4112Combined sources
Helixi42 – 465Combined sources
Helixi47 – 493Combined sources
Helixi57 – 6913Combined sources
Beta strandi71 – 744Combined sources
Helixi76 – 8712Combined sources
Beta strandi94 – 10310Combined sources
Beta strandi109 – 11911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9LX-ray2.90A/B/C/D/E/F/G/H1-120[»]
ProteinModelPortaliP0AC19.
SMRiP0AC19. Positions 2-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC19.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHNA family.Curated

Phylogenomic databases

eggNOGiENOG4105KKP. Bacteria.
COG1539. LUCA.
HOGENOMiHOG000217626.
InParanoidiP0AC19.
KOiK07589.
OMAiTKAIIAH.
OrthoDBiEOG6ND0KG.
PhylomeDBiP0AC19.

Family and domain databases

InterProiIPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 304NNRQ → KQPS in AAB47972 (PubMed:9182560).Curated
Sequence conflicti48 – 492SE → RQ in AAB47972 (PubMed:9182560).Curated
Sequence conflicti55 – 551L → M in AAB47972 (PubMed:9182560).Curated
Sequence conflicti107 – 1071R → A in AAB47972 (PubMed:9182560).Curated

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.
PATRICi32119977. VBIEscCol129921_2398.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9LX-ray2.90A/B/C/D/E/F/G/H1-120[»]
ProteinModelPortaliP0AC19.
SMRiP0AC19. Positions 2-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260518. 7 interactions.
DIPiDIP-9679N.
IntActiP0AC19. 3 interactions.
STRINGi511145.b2303.

Proteomic databases

EPDiP0AC19.
PaxDbiP0AC19.
PRIDEiP0AC19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75363; AAC75363; b2303.
BAA16140; BAA16140; BAA16140.
GeneIDi946781.
KEGGiecj:JW2300.
eco:b2303.
PATRICi32119977. VBIEscCol129921_2398.

Organism-specific databases

EchoBASEiEB4011.
EcoGeneiEG14263. folX.

Phylogenomic databases

eggNOGiENOG4105KKP. Bacteria.
COG1539. LUCA.
HOGENOMiHOG000217626.
InParanoidiP0AC19.
KOiK07589.
OMAiTKAIIAH.
OrthoDBiEOG6ND0KG.
PhylomeDBiP0AC19.

Enzyme and pathway databases

BioCyciEcoCyc:H2NTPEPIM-MONOMER.
ECOL316407:JW2300-MONOMER.
MetaCyc:H2NTPEPIM-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AC19.
PROiP0AC19.

Family and domain databases

InterProiIPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00526. folB_dom. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dihydroneopterin triphosphate epimerase of Escherichia coli: purification, genetic cloning, and expression."
    Haussmann C., Rohdich F., Lottspeich F., Eberhardt S., Scheuring J., Mackamul S., Bacher A.
    J. Bacteriol. 179:949-951(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / RR28.
  2. "Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli."
    Ahn C., Byun J., Yim J.
    J. Biol. Chem. 272:15323-15328(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Haussmann C., Bacher A.
    Submitted (MAY-1995) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-22.
    Strain: DSM 613.
  7. "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase."
    Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.
    J. Biol. Chem. 273:17418-17424(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, REACTION MECHANISM.
  8. "FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa."
    Pribat A., Blaby I.K., Lara-Nunez A., Gregory J.F., de Crecy-Lagard V., Hanson A.D.
    J. Bacteriol. 192:475-482(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Crystal structure of 7,8-dihydroneopterin triphosphate epimerase."
    Ploom T., Haussmann C., Hof P., Steinbacher S., Bacher A., Richardson J., Huber R.
    Structure 7:509-516(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiFOLX_ECOLI
AccessioniPrimary (citable) accession number: P0AC19
Secondary accession number(s): P77796, P80449
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 88 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.