P51594 (GCH1_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 190 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 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. |
| Sequence caution | The sequence CAA59929.1 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase I activityInferred from electronic annotation. Source: EC metal ion bindingInferred 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
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References
| « Hide '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. 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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X85954 Genomic DNA. Translation: CAA59929.1. Different initiation. AL111168 Genomic DNA. Translation: CAL34363.1. |
| PIR | A81438. I40754. |
| RefSeq | YP_002343652.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | P51594. |
| SMR | P51594. Positions 2-183. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P51594. 1 interaction. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 904536. |
| GenomeReviews | Gene locus Cj0194 in contig AL111168_GR. |
| KEGG | cje:Cj0194. |
| PATRIC | 20057315. VBICamJej33762_0191. |
Phylogenomic databases | |
| HOGENOM | HBG370191. |
| OMA | LPFMGRA. |
| ProtClustDB | PRK09347. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0194-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00223. FolE. [Tree] |
| InterPro | IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view] |
| KO | K01495. |
| PANTHER | PTHR11109. GTP_cyclohydro_I. 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. 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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