Reviewed,
UniProtKB/Swiss-Prot Q5LT54 (FOLD2_SILPO)
Last modified
January 19, 2010.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional protein folD 2 Including the following 2 domains: 1- Recommended name: Methylenetetrahydrofolate dehydrogenase EC=1.5.1.5 2- Recommended name: Methenyltetrahydrofolate cyclohydrolase EC=3.5.4.9 | ||||
| Gene names |
| ||||
| Organism | Silicibacter pomeroyi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 89184 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria |
Protein attributes
| Sequence length | 292 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate By similarity. HAMAP MF_01576 |
| Catalytic activity | 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP MF_01576 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP MF_01576 |
| Pathway | One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_01576 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01576 |
| Sequence similarities | Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 292 | 292 | Bifunctional protein folD 2 HAMAP MF_01576 | PRO_0000268502 | |||
Sequences
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References
| [1] | "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. Ward N.Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000031 Genomic DNA. Translation: AAV94847.1. |
| RefSeq | YP_166801.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A4I based on UniProtKB P11586. |
| SMR | Q5LT54. Positions 8-285. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3193492. |
| GenomeReviews | Gene locus SPO1560 in contig CP000031_GR. |
| KEGG | sil:SPO1560. |
| NMPDR | fig|246200.3.peg.1970. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG328751. |
| OMA | SIGNIVY. |
Enzyme and pathway databases | |
| BioCyc | RPOM246200:SPO_1560-MONOMER. |
| BRENDA | 1.5.1.5. 278247. 3.5.4.9. 278247. |
Family and domain databases | |
| HAMAP | MF_01576. THF_DHG_CYH. [Tree] |
| InterPro | IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. IPR020630. THF_DH/CycHdrlase_cat_dom. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view] |
| PRINTS | PR00085. THFDHDRGNASE. |
| PROSITE | PS00766. THF_DHG_CYH_1. False negative. PS00767. THF_DHG_CYH_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FOLD2_SILPO | ||||||||
| Accession | Primary (citable) accession number: Q5LT54 | ||||||||
| 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


