Reviewed,
UniProtKB/Swiss-Prot Q9PHU4 (RIBB_CAMJE)
Last modified
June 16, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 3,4-dihydroxy-2-butanone 4-phosphate synthase Short name=DHBP synthase EC=4.1.99.12 | ||||
| Gene names |
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| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. |
| Catalytic activity | D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180 |
| Cofactor | Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. |
| Pathway | Cofactor biosynthesis; riboflavin biosynthesis; 3,4-dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180 |
| Sequence similarities | In the N-terminal section; belongs to the DHBP synthase family. In the C-terminal section; belongs to the GTP cyclohydrolase II family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Riboflavin biosynthesis |
| Ligand | Magnesium Manganese Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP GTP cyclohydrolase II activityInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: HAMAP protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 339 | 339 | 3,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180 | PRO_0000151722 | |||||
Regions | |||||||||
| Region | 1 – 206 | 206 | DHBP synthase HAMAP MF_00180 | ||||||
| Region | 27 – 28 | 2 | Substrate binding By similarity | ||||||
| Region | 139 – 143 | 5 | Substrate binding By similarity | ||||||
| Region | 207 – 339 | 133 | GTP cyclohydrolase II-like HAMAP MF_00180 | ||||||
Sites | |||||||||
| Metal binding | 28 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 28 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 142 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Binding site | 32 | 1 | Substrate By similarity | ||||||
| Binding site | 163 | 1 | Substrate By similarity | ||||||
| Site | 125 | 1 | Essential for catalytic activity By similarity | ||||||
| Site | 163 | 1 | Essential for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "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. |
Cross-references
Sequence databases | |
|---|---|
| AL111168 Genomic DNA. Translation: CAL34718.1. | |
| PIR | C81404. |
| RefSeq | YP_002344002.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1G58 based on UniProtKB P24199. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PHU4. 69 interactions. |
Genome annotation databases | |
| GeneID | 904897. |
| GenomeReviews | Gene locus Cj0572 in contig AL111168_GR. |
| KEGG | cje:Cj0572. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | Q9PHU4. ISELMND. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0572-MON. |
| BRENDA | 4.1.99.12. 255835. |
Family and domain databases | |
| HAMAP | MF_00180. Fused. [Tree] |
| InterPro | IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlase_II. IPR016299. Riboflavin_synth_RibA. [Graphical view] |
| Gene3D | G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit. |
| Pfam | PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view] |
| PIRSF | PIRSF001259. RibA. 1 hit. |
| ProDom | PD003034. DHBP_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00506. ribB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RIBB_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PHU4 Secondary accession number(s): Q0PAU5 | ||||||||
| 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 |

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