P0C0C2 (GCH1_STRP1) 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:	SPy_1097, M5005_Spy0821

Organism

Streptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]

Taxonomic identifier

301447 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes

Protein attributes

Sequence length	194 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 AAK33975.1 differs from that shown. Reason: Erroneous initiation. The sequence AAZ51439.1 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 – 194	194	GTP cyclohydrolase 1 HAMAP-Rule MF_00223		PRO_0000119452
Sites
	Metal binding	83	1	Zinc By similarity
	Metal binding	86	1	Zinc By similarity
	Metal binding	155	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C0C2 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 03675C972EED7A0F	FASTA	194	21,871
	10 20 30 40 50 60 MKRERLMSIN KEKAEAAIYQ FLEAIGENPN REGLLDTPKR VAKMYAEMFL GLGKDPKEEF 70 80 90 100 110 120 TAVFKEQHED VVIVKDISFY SICEHHLVPF YGKAHIAYLP SDGRVTGLSK LARAVEVASK 130 140 150 160 170 180 RPQLQERLTS QIADALVEAL NPKGTLVMVE AEHMCMTMRG IKKPGSKTIT TTARGLYKES 190 RAERQEVISL MTKD

References

[1]

"Complete genome sequence of an M1 strain of Streptococcus pyogenes." Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E. Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700294 / SF370 / Serotype M1.

[2]

"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events." Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M. J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004092 Genomic DNA. Translation: AAK33975.1. Different initiation. CP000017 Genomic DNA. Translation: AAZ51439.1. Different initiation.
RefSeq	NP_269254.1. NC_002737.1. YP_282184.1. NC_007297.1.
3D structure databases
ProteinModelPortal	P0C0C2.
ModBase	Search...
Protein-protein interaction databases
STRING	160490.SPy_1097.
Proteomic databases
PaxDb	P0C0C2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK33975; AAK33975; SPy_1097. AAZ51439; AAZ51439; M5005_Spy0821.
GeneID	3572069. 901218.
KEGG	spy:SPy_1097. spz:M5005_Spy_0821.
PATRIC	19715777. VBIStrPyo79812_0953.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0302.
HOGENOM	HOG000221222.
KO	K01495.
OMA	KEHHEDV.
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_STRP1

Accession

Primary (citable) accession number: P0C0C2
Secondary accession number(s): O33723 , P0A3E8, Q48YY3, Q8P153

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program