HAMAP rule MF_01268
General rule information
[?]
| Accession | MF_01268 |
| Dates | 2-MAY-2006 (Created)
1-JUN-2023 (Last updated, Version 18) |
| Name | Fae_Hps |
| Scope(s) |
Archaea |
| Template(s) | Q46DY5 (FAEHP_METBF); Q58842 (FAEHP_METJA); [ Recover all ] |
| Triggered by |
HAMAP; MF_01268 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier | FAEHP |
| Protein name | RecName: Full=Bifunctional enzyme Fae/Hps; Includes: RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase; EC=4.2.1.147; AltName: Full=Formaldehyde-activating enzyme; Short=Fae; Includes: RecName: Full=3-hexulose-6-phosphate synthase; Short=HPS; EC=4.1.2.43; AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase; |
| Gene name | Name=fae-hps; |
Comments
[?]
| FUNCTION | Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10- methylenetetrahydromethanopterin. |
| FUNCTION | Catalyzes the reversible formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. |
| CATALYTIC ACTIVITY | Reaction=5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10- methylenetetrahydromethanopterin + H2O; Xref=Rhea:RHEA:24678, ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:57818, ChEBI:CHEBI:58103; EC=4.2.1.147; |
| CATALYTIC ACTIVITY | Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose 6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842, ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43; |
| PATHWAY | Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis. |
| SIMILARITY | In the N-terminal section; belongs to the formaldehyde- activating enzyme family. |
| SIMILARITY | In the C-terminal section; belongs to the HPS/KGPDC family. HPS subfamily. |
Keywords
[?]
Gene Ontology
[?]
| GO:0043801; Molecular function:hexulose-6-phosphate synthase activity |
| GO:0016836; Molecular function:hydro-lyase activity |
| GO:0016051; Biological process:carbohydrate biosynthetic process |
Cross-references
[?]
Features
[?]
| From: FAEHP_METBF (Q46DY5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | Nter | 161 | /note="Formaldehyde-activating enzyme" | |||||||||
| REGION | 162 | Cter | /note="3-hexulose-6-phosphate synthase" | |||||||||
| ACT_SITE | 17 | 17 | /note="Proton donor" | H | ||||||||
| BINDING | 19 | 19 | /ligand="substrate" | D | ||||||||
| BINDING | 48 | 48 | /ligand="substrate" | L | ||||||||
| BINDING | 66 | 66 | /ligand="substrate" | K | ||||||||
| BINDING | 68 | 68 | /ligand="substrate" | T | ||||||||
| BINDING | 83 | 83 | /ligand="substrate" | Q | ||||||||
Additional information
[?]
| Size range | 375-420 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | In METJA, lacks the active site His and substrate binding sites expected to be involved in fae activity. Monofunctional fae enzyme exists in methylotrophic bacteria, where it is involved in energy metabolism and formaldehyde detoxification. Monofunctional HPS enzyme exists in bacteria, but functions in the opposite direction (condensation of ribulose 5-phosphate with formaldehyde), and is involved in C1 assimilation and/or formaldehyde detoxification. METBF possesses the bifunctional fae/hps enzyme, and also the two monofunctional enzymes fae and hps. FT lines are propagated from Methylobacterium extorquens fae enzyme, whose X-ray structure is known. |