GTP cyclohydrolase-2 - Escherichia coli (strain K12)

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P0A7I7 (RIBA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	b1277, JW1269

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. Ref.6
Catalytic activity	GTP + 3 H₂O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP-Rule MF_00179
Cofactor	Binds 1 zinc ion per subunit. Ref.6 Ref.8
Enzyme regulation	Competitively inhibited by pyrophosphate. Ref.6 Ref.7
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP-Rule MF_00179
Subunit structure	Homodimer. Ref.6
Miscellaneous	Catalyzes the formation of GMP as minor product, with concomitant release of pyrophosphate. Release of pyrophosphate requires magnesium ions. HAMAP-Rule MF_00179
Sequence similarities	Belongs to the GTP cyclohydrolase II family.
Biophysicochemical properties	Kinetic parameters: K_M=41 µM for GTP Ref.6 pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	GTP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase II activity Inferred from direct assay Ref.1. Source: EcoCyc zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pyrF	P08244	2	EBI-1123314,EBI-1123202

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

GTP cyclohydrolase-2 HAMAP-Rule MF_00179

PRO_0000151754

Regions

Nucleotide binding

49 – 53

GTP HAMAP-Rule MF_00179

Nucleotide binding

92 – 94

GTP HAMAP-Rule MF_00179

Sites

Active site

126

Proton acceptor Potential

Active site

128

Nucleophile

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Binding site

GTP

Binding site

114

GTP

Binding site

149

GTP

Binding site

154

GTP

Experimental info

Mutagenesis

C → S: Loss of zinc binding. Loss of ring-opening activity. Can still remove phosphate from GTP. Ref.8

Mutagenesis

C → S: Loss of zinc binding. Loss of ring-opening activity. Can still remove phosphate from GTP. Ref.8

Mutagenesis

C → S: Loss of zinc binding. Loss of ring-opening activity. Can still remove phosphate from GTP. Ref.8

Secondary structure

196

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7I7 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: C22FED98F48098DF
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FASTA

196

21,836

        10         20         30         40         50         60 
MQLKRVAEAK LPTPWGDFLM VGFEELATGH DHVALVYGDI SGHTPVLARV HSECLTGDAL 

        70         80         90        100        110        120 
FSLRCDCGFQ LEAALTQIAE EGRGILLYHR QEGRNIGLLN KIRAYALQDQ GYDTVEANHQ 

       130        140        150        160        170        180 
LGFAADERDF TLCADMFKLL GVNEVRLLTN NPKKVEILTE AGINIVERVP LIVGRNPNNE 

       190 
HYLDTKAEKM GHLLNK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biosynthesis of riboflavin: cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II in Escherichia coli." Richter G., Ritz H., Katzenmeier G., Volk R., Kohnle A., Lottspeich F., Allendorf D., Bacher A. J. Bacteriol. 175:4045-4051(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases." Prodromou C., Artymiuk P.J., Guest J.R. Eur. J. Biochem. 204:599-609(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-196.
[6]	"Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli." Foor F., Brown G.M. J. Biol. Chem. 250:3545-3551(1975) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION, COFACTOR.
[7]	"Biosynthesis of riboflavin: studies on the mechanism of GTP cyclohydrolase II." Ritz H., Schramek N., Bracher A., Herz S., Eisenreich W., Richter G., Bacher A. J. Biol. Chem. 276:22273-22277(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME MECHANISM, ENZYME REGULATION.
[8]	"Biosynthesis of vitamin B2." Kaiser J., Schramek N., Eberhardt S., Puettmer S., Schuster M., Bacher A. Eur. J. Biochem. 269:5264-5270(2002) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, MUTAGENESIS OF CYS-54; CYS-65 AND CYS-67.
[9]	"GTP cyclohydrolase II structure and mechanism." Ren J., Kotaka M., Lockyer M., Lamb H.K., Hawkins A.R., Stammers D.K. J. Biol. Chem. 280:36912-36919(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH GTP ANALOG AND ZINC IONS, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67876 Genomic DNA. Translation: CAA48075.1.
U00096 Genomic DNA. Translation: AAC74359.1.
AP009048 Genomic DNA. Translation: BAA14831.1.
X60293 Genomic DNA. Translation: CAA42835.1.

PIR

A40654.

RefSeq

NP_415793.1. NC_000913.2.
YP_489545.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BZ0	X-ray	2.60	A/B	1-196	[»]
2BZ1	X-ray	1.54	A	1-196	[»]

ProteinModelPortal

P0A7I7.

SMR

P0A7I7. Positions 1-173.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36049N.

IntAct

P0A7I7. 2 interactions.

STRING

511145.b1277.

Proteomic databases

PaxDb

P0A7I7.

PRIDE

P0A7I7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74359; AAC74359; b1277.
BAA14831; BAA14831; BAA14831.

GeneID

12934365.
945763.

KEGG

ecj:Y75_p1252.
eco:b1277.

PATRIC

32117816. VBIEscCol129921_1328.

Organism-specific databases

EchoBASE

EB1307.

EcoGene

EG11331. ribA.

Phylogenomic databases

eggNOG

COG0807.

HOGENOM

HOG000115442.

K01497.

OMA

QGFILYL.

ProtClustDB

PRK00393.

Enzyme and pathway databases

BioCyc

EcoCyc:GTP-CYCLOHYDRO-II-MONOMER.
ECOL316407:JW1269-MONOMER.
MetaCyc:GTP-CYCLOHYDRO-II-MONOMER.

UniPathway

UPA00275; UER00400.

Gene expression databases

Genevestigator

P0A7I7.

Family and domain databases

HAMAP

MF_00179. RibA.

InterPro

IPR000926. GTP_CycHdrlaseII_RibA.
[Graphical view]

Pfam

PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00505. ribA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7I7.

Entry information

Entry name

RIBA_ECOLI

Accession

Primary (citable) accession number: P0A7I7
Secondary accession number(s): P25523, P78147

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents