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Q5F9K6 (GCH4_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase FolE2

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase 1B
Gene names
Name:folE2
Ordered Locus Names:NGO0387
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts GTP to 7,8-dihydroneopterin triphosphate. Ref.2

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. Ref.2

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_01527_B

Sequence similarities

Belongs to the GTP cyclohydrolase IV family.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7,8-dihydroneopterin 3'-triphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionGTP cyclohydrolase I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257GTP cyclohydrolase FolE2 HAMAP-Rule MF_01527_B
PRO_0000147714

Sites

Site1471May be catalytically important By similarity

Secondary structure

.................................. 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5F9K6 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: A0235399C3EDF2A9

FASTA25728,747
        10         20         30         40         50         60 
MNAIADVQSS RDLRNLPINQ VGIKDLRFPI TLKTAEGTQS TVARLTMTVY LPAEQKGTHM 

        70         80         90        100        110        120 
SRFVALMEQH TEVLDFAQLH RLTAEMVALL DSRAGKISVS FPFFRKKTAP VSGIRSLLDY 

       130        140        150        160        170        180 
DVSLTGEMKD GAYGHSMKVM IPVTSLCPCS KEISQYGAHN QRSHVTVSLT SDAEVGIEEV 

       190        200        210        220        230        240 
IDYVETQASC QLYGLLKRPD EKYVTEKAYE NPKFVEDMVR DVATSLIADK RIKSFVVESE 

       250 
NFESIHNHSA YAYIAYP 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.
[2]"Discovery of a new prokaryotic type I GTP cyclohydrolase family."
El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., Iwata-Reuyl D., de Crecy-Lagard V.
J. Biol. Chem. 281:37586-37593(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW89131.1.
RefSeqYP_207543.1. NC_002946.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D1TX-ray2.20A/B1-257[»]
3D2OX-ray2.04A/B1-257[»]
ProteinModelPortalQ5F9K6.
SMRQ5F9K6. Positions 15-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO0387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW89131; AAW89131; NGO0387.
GeneID3282560.
KEGGngo:NGO0387.
PATRIC20333781. VBINeiGon24812_0468.

Phylogenomic databases

eggNOGCOG1469.
HOGENOMHOG000280679.
KOK09007.
OMAINMYVDL.
OrthoDBEOG6X6RBH.
ProtClustDBPRK13674.

Enzyme and pathway databases

BioCycNGON242231:GI2G-366-MONOMER.
UniPathwayUPA00848; UER00151.

Family and domain databases

HAMAPMF_01527_B. GTP_cyclohydrol_B.
InterProIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00294. TIGR00294. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ5F9K6.

Entry information

Entry nameGCH4_NEIG1
AccessionPrimary (citable) accession number: Q5F9K6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways