O08315 (RIBA_HELPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTP cyclohydrolase-2
EC=3.5.4.25

Alternative name(s):
GTP cyclohydrolase II

Gene names

Name:	ribA
Ordered Locus Names:	HP_0802

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate Probable. HAMAP MF_00179
Catalytic activity	GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP MF_00179
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00179
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP MF_00179
Sequence similarities	Belongs to the GTP cyclohydrolase II family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase II activity Inferred from electronic annotation. Source: EC metal 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 – 192	192	GTP cyclohydrolase-2 HAMAP MF_00179		PRO_0000151761
Regions
	Nucleotide binding	50 – 54	5	GTP By similarity
	Nucleotide binding	92 – 94	3	GTP By similarity
Sites
	Active site	126	1	Proton acceptor Potential
	Active site	128	1	Nucleophile By similarity
	Metal binding	55	1	Zinc; catalytic By similarity
	Metal binding	66	1	Zinc; catalytic By similarity
	Metal binding	68	1	Zinc; catalytic By similarity
	Binding site	114	1	GTP By similarity
	Binding site	149	1	GTP By similarity
	Binding site	154	1	GTP By similarity
Experimental info
	Sequence conflict	38	1	V → I in CAA72785. Ref.2
	Sequence conflict	44	1	S → P in CAA72785. Ref.2
	Sequence conflict	72	1	L → F in CAA72785. Ref.2
	Sequence conflict	75	1	A → P in CAA72785. Ref.2
	Sequence conflict	98 – 100	3	LFN → YLT Ref.2
	Sequence conflict	102	1	V → S Ref.2
	Sequence conflict	141	1	R → H in CAA72785. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O08315 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1F34B0E1FC3A73A4	FASTA	192	21,715
	10 20 30 40 50 60 MKRLEVSNQA KLPTQFGEFY IQCFREKGSN GSKDHLVVFT PNFSQNPLVR LHSECLTGDA 70 80 90 100 110 120 LGSQKCDCGG ALQMALERIS KEGGLVIYLR QEGRGIGLFN KVNAYALQDK GYDTIQANEM 130 140 150 160 170 180 IGFKDDERDY SVAGEILEYY RIKKMRLLTN NPKKIAALEK YAEVTRESLI VCANEHNQGY 190 LEVKKLKMGH LL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[2]	"Hemolytic properties and riboflavin synthesis of Helicobacter pylori: cloning and functional characterization of the ribA gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli." Bereswill S., Fassbinder F., Voelzing C., Covacci A., Haas R., Kist M. Med. Microbiol. Immunol. 186:177-187(1998) [PubMed: 9574900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 4867 / CCUG 17874 / NCTC 11638.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD07851.1. Y12062 Genomic DNA. Translation: CAA72785.1.
PIR	B64620.
RefSeq	NP_207595.1. NC_000915.1.
3D structure databases
ProteinModelPortal	O08315.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3449N.
MINT	MINT-160492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	899351.
GenomeReviews	Gene locus HP_0802 in contig AE000511_GR.
KEGG	hpy:HP0802.
NMPDR	fig|85962.1.peg.793.
PATRIC	20592891. VBIHelPyl33062_0834.
TIGR	HP_0802.
Phylogenomic databases
HOGENOM	HBG735778.
OMA	IKPNKFN.
ProtClustDB	PRK00393.
Family and domain databases
HAMAP	MF_00179. RibA. [Tree]
InterPro	IPR000926. GTP_CycHdrlaseII_RibA. [Graphical view]
KO	K01497.
Pfam	PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00505. RibA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBA_HELPY

Accession

Primary (citable) accession number: O08315

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program