P64207 (GCH1_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 62.
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 | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 202 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-Rule MF_00223 |
| Pathway | Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. HAMAP-Rule 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway growthInferred from mutant phenotype PubMed 12657046. Source: MTBBASE one-carbon metabolic processInferred 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 202 | 202 | GTP cyclohydrolase 1 HAMAP-Rule MF_00223 | PRO_0000119423 | |||||
Sites | |||||||||
| Metal binding | 90 | 1 | Zinc By similarity | ||||||
| Metal binding | 93 | 1 | Zinc By similarity | ||||||
| Metal binding | 163 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842583 Genomic DNA. Translation: CAB08935.1. AE000516 Genomic DNA. Translation: AAK48072.1. AL123456 Genomic DNA. Translation: CCP46432.1. |
| PIR | B70956. |
| RefSeq | NP_218126.1. NC_000962.3. NP_338258.1. NC_002755.2. YP_006517098.1. NC_018143.1. |
3D structure databases | |
| ProteinModelPortal | P64207. |
| SMR | P64207. Positions 23-199. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 83332.Rv3609c. |
Proteomic databases | |
| PRIDE | P64207. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAK48072; AAK48072; MT3713. |
| GeneID | 13317217. 885346. 922777. |
| KEGG | mtc:MT3713. mtu:Rv3609c. mtv:RVBD_3609c. |
| PATRIC | 18129919. VBIMycTub22151_4054. |
Organism-specific databases | |
| TubercuList | Rv3609c. |
Phylogenomic databases | |
| eggNOG | COG0302. |
| HOGENOM | HOG000221222. |
| KO | K01495. |
| OMA | LIRHQPA. |
| ProtClustDB | PRK09347. |
Enzyme and pathway databases | |
| UniPathway | UPA00848; UER00151. |
Family and domain databases | |
| HAMAP | MF_00223. FolE. |
| InterPro | IPR001474. GTP_CycHdrlase_I. IPR020602. GTP_CycHdrlase_I/CN_OxRdtase. IPR018234. GTP_CycHdrlase_I_CS. [Graphical view] |
| PANTHER | PTHR11109. PTHR11109. 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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P64207 Secondary accession number(s): L0TEP6, O06273 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
