Reviewed,
UniProtKB/Swiss-Prot A5I231 (GCH1_CLOBH)
Last modified
November 3, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
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| Organism | Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 441771 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 196 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
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 | one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP tetrahydrofolate biosynthetic processInferred 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 activityInferred from electronic annotation. Source: HAMAP zinc 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 – 196 | 196 | GTP cyclohydrolase 1 HAMAP MF_00223 | PRO_1000043679 | |||||
Sites | |||||||||
| Metal binding | 86 | 1 | Zinc By similarity | ||||||
| Metal binding | 89 | 1 | Zinc By similarity | ||||||
| Metal binding | 158 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. Parkhill J.Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000727 Genomic DNA. Translation: ABS36547.1. AM412317 Genomic DNA. Translation: CAL83096.1. | |
| RefSeq | YP_001254064.1. YP_001387448.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5I231. |
Genome annotation databases | |
| GeneID | 5185811. 5399029. |
| GenomeReviews | Gene locus CBO1556 in contig AM412317_GR. Gene locus CLC_1588 in contig CP000727_GR. |
| KEGG | cbh:CLC_1588. cbo:CBO1556. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | ILPIIGR. |
Family and domain databases | |
| HAMAP | MF_00223. [Tree] |
| InterPro | IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view] |
| PANTHER | PTHR11109. GTP_cyclohydro_I. 1 hit. |
| Pfam | PF01227. GTP_cyclohydroI. 1 hit. [Graphical view] |
| ProDom | PD003330. GTP_cyclohydroI. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| 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_CLOBH | ||||||||
| Accession | Primary (citable) accession number: A5I231 Secondary accession number(s): A7G3T3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


