Reviewed, UniProtKB/Swiss-Prot P51594 (GCH1_CAMJE)

Names and origin

Protein names

Recommended name:
    GTP cyclohydrolase 1
    EC=3.5.4.16
Alternative name(s):
    GTP cyclohydrolase I
      Short name=GTP-CH-I

Gene names

Name:	folE
Ordered Locus Names:	Cj0194

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. HAMAP MF_00223
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP MF_00223
Subunit structure	Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.
Sequence similarities	Belongs to the GTP cyclohydrolase I family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	GTP cyclohydrolase 1 HAMAP MF_00223		PRO_0000119393
Sites
	Metal binding	75	1	Zinc By similarity
	Metal binding	78	1	Zinc By similarity
	Metal binding	146	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51594-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 24B4CC39BEA49564	FASTA	190	21,800
	10 20 30 40 50 60 MQKKFEDCVK TMLEIIGENP NREGLIKTPN RVFKAYEFLT SGYTQNVKEI LNDALFESSN 70 80 90 100 110 120 NEMVLVRDIE FYSLCEHHLL PFFGRAHVAY IPNKKVVGLS KIPRLVEVFA RRLQIQEQLT 130 140 150 160 170 180 EQIAQALMEN VDAKGVGVVI EARHMCVEMR GVQKANSTTT TSALRGIFLK NEKTREEFFS 190 LINSAKQVRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene for Campylobacter trigger factor: evidence for multiple transcription start sites and protein products." Griffiths P.L., Park R.W.A., Connerton I.F. Microbiology 141:1359-1367(1995) [PubMed: 7670637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
[2]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X85954 Genomic DNA. Translation: CAA59929.1. Different initiation. AL111168 Genomic DNA. Translation: CAL34363.1.
PIR	A81438. I40754.
RefSeq	YP_002343652.1.
3D structure databases
HSSP	HSSP built from PDB template 1IS8 based on UniProtKB P22288.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51594. 1 interaction.
Genome annotation databases
GeneID	904536.
GenomeReviews	Gene locus Cj0194 in contig AL111168_GR.
KEGG	cje:Cj0194.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P51594.
OMA	RITSTIA.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0194-MON.
BRENDA	3.5.4.16. 255835.
Family and domain databases
HAMAP	MF_00223. [Tree]
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
PANTHER	PTHR11109. GTP_cyclohydro_I. 1 hit.
Pfam	PF01227. GTP_cyclohydroI. 1 hit. [Graphical view]
ProDom	PD003330. GTP_cyclohydroI. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00063. folE. 1 hit.
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCH1_CAMJE

Accession

Primary (citable) accession number: P51594
Secondary accession number(s): Q0PBU5, Q9PIT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)