Q8PEP3 (GCH1_XANAC) Reviewed, UniProtKB/Swiss-Prot

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:	XAC4302

Organism

Xanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]

Taxonomic identifier

190486 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas citri group › Xanthomonas campestris pv. citri › Xanthomonas citri pv. citri

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
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-Rule MF_00223
Pathway	Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule 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.
Sequence caution	The sequence AAM39132.1 differs from that shown. Reason: Erroneous initiation.

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	7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 200	200	GTP cyclohydrolase 1 HAMAP-Rule MF_00223		PRO_0000119466
Sites
	Metal binding	87	1	Zinc By similarity
	Metal binding	90	1	Zinc By similarity
	Metal binding	158	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PEP3 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: AF91D4AF9D14D802	FASTA	200	22,626
	10 20 30 40 50 60 MSQSNQPDSP VTQTQAEEAV RTLLRWAGED PTREGLLDTP RRVAEAYGDW FSGYRDEPRE 70 80 90 100 110 120 YLERTFEEVA GYDELIVLRD ISYESHCEHH MAPIIGKVHV GYLPRGKVVG ISKLARVVES 130 140 150 160 170 180 YARRFQVQEK MTAQIAQCIQ DVLQPLGVGV VVEGAHECMT TRGIHKRGVS MVTSKMLGSF 190 200 REDARTRAEF LQFIEVGGKR

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM39132.1. Different initiation.
RefSeq	NP_644596.1. NC_003919.1.
3D structure databases
ProteinModelPortal	Q8PEP3.
ModBase	Search...
Protein-protein interaction databases
STRING	190486.XAC4302.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM39132; AAM39132; XAC4302.
GeneID	1158373.
KEGG	xac:XAC4302.
PATRIC	24060804. VBIXanAxo33670_4440.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0302.
HOGENOM	HOG000221222.
KO	K01495.
OMA	EPREYLE.
ProtClustDB	PRK09347.
Enzyme and pathway databases
UniPathway	UPA00848; UER00151.
Family and domain databases
HAMAP	MF_00223. FolE.
InterPro	IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view]
PANTHER	PTHR11109. PTHR11109. 1 hit.
Pfam	PF01227. GTP_cyclohydroI. 1 hit. [Graphical view]
TIGRFAMs	TIGR00063. folE. 1 hit.
PROSITE	PS00859. GTP_CYCLOHYDROL_1_1. 1 hit. PS00860. GTP_CYCLOHYDROL_1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCH1_XANAC

Accession

Primary (citable) accession number: Q8PEP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	November 15, 2002
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program