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Q65ML7 (GCH4_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:folE2
Ordered Locus Names:BLi00762, BL02349
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts GTP to 7,8-dihydroneopterin triphosphate By similarity. HAMAP-Rule MF_01527

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP-Rule MF_01527

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule MF_01527

Sequence similarities

Belongs to the GTP cyclohydrolase IV family.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termComplete 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 – 300300GTP cyclohydrolase FolE2 HAMAP-Rule MF_01527
PRO_0000147700

Sites

Site1831May be catalytically important By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65ML7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: A23E6D14EB8E1CF6

FASTA30034,080
        10         20         30         40         50         60 
MERKLHLPAK PERHRRFGSV EAVKGIKPTD KEQMKDIQNT PNDYFFDIDH VGVSNVSHPI 

        70         80         90        100        110        120 
LIASSLKPFT QTTIGAFSFT TSLARDRKGI NMSRLTEQLQ RYHEANWTVD FHTLKDFAKD 

       130        140        150        160        170        180 
LAGNMEQESA SVSVSFPWYF ERISPETKLS GLMHADIHMT VSYHENKGFS QTAGITAHAT 

       190        200        210        220        230        240 
TLCPCSKEIS EYSAHNQRGI IKITAHINEQ AEMPDDFKAE LLAAAETNAS AKLHPVLKRP 

       250        260        270        280        290        300 
DEKRVTEQAY ENPRFVEDVL RLTAADLYEM DWISAFEIEC RNEESIHLHD AVARLSFSKC 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU39697.1.
CP000002 Genomic DNA. Translation: AAU22347.1.
RefSeqYP_006712167.1. NC_006322.1.
YP_077985.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65ML7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL02349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22347; AAU22347; BL02349.
AAU39697; AAU39697; BLi00762.
GeneID3031477.
3098927.
KEGGbld:BLi00762.
bli:BL02349.
PATRIC18947055. VBIBacLic203714_0752.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1469.
HOGENOMHOG000280679.
KOK09007.
OMADVQSSRD.
OrthoDBEOG6X6RBH.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-755-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...

Entry information

Entry nameGCH4_BACLD
AccessionPrimary (citable) accession number: Q65ML7
Secondary accession number(s): Q62Y11
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 60 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

PATHWAY comments

Index of metabolic and biosynthesis pathways