Q8NM84 (GCH1_CORGL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 60.
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 |
| ||||
| Organism | Corynebacterium glutamicum (Brevibacterium flavum) | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 196 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 CAF20718.1 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 – 196 | 196 | GTP cyclohydrolase 1 HAMAP MF_00223 | PRO_0000119401 | |||||
Sites | |||||||||
| Metal binding | 84 | 1 | Zinc By similarity | ||||||
| Metal binding | 87 | 1 | Zinc By similarity | ||||||
| Metal binding | 157 | 1 | Zinc By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [2] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000036 Genomic DNA. Translation: BAC00089.1. BX927156 Genomic DNA. Translation: CAF20718.1. Different initiation. |
| RefSeq | NP_601891.1. NC_003450.3. YP_226934.1. NC_006958.1. |
3D structure databases | |
| ProteinModelPortal | Q8NM84. |
| SMR | Q8NM84. Positions 9-194. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1020642. 3344752. |
| GenomeReviews | Gene locus Cgl2695 in contig BA000036_GR. Gene locus cg2983 in contig BX927147_GR. |
| KEGG | cgb:cg2983. cgl:NCgl2602. |
| PATRIC | 21497430. VBICorGlu203724_2627. |
Phylogenomic databases | |
| HOGENOM | HBG370191. |
| OMA | LPFMGRA. |
| PhylomeDB | Q8NM84. |
| ProtClustDB | PRK09347. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:CG2983-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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GCH1_CORGL | ||||||||
| Accession | Primary (citable) accession number: Q8NM84 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with