Reviewed,
UniProtKB/Swiss-Prot Q1AT41 (FOLD3_RUBXD)
Last modified
January 19, 2010.
Version 28.
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 3 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 | Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 266117 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Rubrobacteridae › Rubrobacterales › Rubrobacterineae › Rubrobacteraceae › Rubrobacter |
Protein attributes
| Sequence length | 318 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 – 318 | 318 | Bifunctional protein folD 3 HAMAP MF_01576 | PRO_0000268487 | |||
Sequences
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References
| [1] | "Complete sequence of Rubrobacter xylanophilus DSM 9941." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. Richardson P.Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000386 Genomic DNA. Translation: ABG05437.1. |
| RefSeq | YP_645249.1. |
3D structure databases | |
| SMR | Q1AT41. Positions 2-296. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1AT41. |
Genome annotation databases | |
| GeneID | 4117102. |
| GenomeReviews | Gene locus Rxyl_2517 in contig CP000386_GR. |
| KEGG | rxy:Rxyl_2517. |
| NMPDR | fig|266117.6.peg.2194. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0190. |
| HOGENOM | HBG328751. |
| OMA | LLASHIV. |
Enzyme and pathway databases | |
| BioCyc | RXYL266117:RXYL_2517-MONOMER. |
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 | FOLD3_RUBXD | ||||||||
| Accession | Primary (citable) accession number: Q1AT41 | ||||||||
| 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


