Q46DY5 (FAEHP_METBF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 51.
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: Bifunctional enzyme fae/hps | ||||
| Gene names |
| ||||
| Organism | Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 269797 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina › ![]() |
Protein attributes
| Sequence length | 392 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H4MPT) to 5,10-methylenetetrahydromethanopterin. Ref.2 Catalyzes the formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. Ref.2 |
| Catalytic activity | 5,10-methylenetetrahydromethanopterin = tetrahydromethanopterin + formaldehyde. HAMAP-Rule MF_01268 D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde. HAMAP-Rule MF_01268 |
| Pathway | Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis. Ref.2 |
| Sequence similarities | In the N-terminal section; belongs to the formaldehyde-activating enzyme family. In the C-terminal section; belongs to the HPS/KGPDC family. HPS subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Molecular function | Lyase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological_process | 'de novo' pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro carbohydrate biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular_function | aldehyde-lyase activity Inferred from electronic annotation. Source: HAMAP carbon-nitrogen lyase activityInferred from electronic annotation. Source: HAMAP orotidine-5'-phosphate decarboxylase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 392 | 392 | Bifunctional enzyme fae/hps HAMAP-Rule MF_01268 | PRO_0000235168 | |||||
Regions | |||||||||
| Region | 1 – 161 | 161 | Formaldehyde-activating enzyme HAMAP-Rule MF_01268 | ||||||
| Region | 162 – 392 | 231 | 3-hexulose-6-phosphate synthase HAMAP-Rule MF_01268 | ||||||
Sites | |||||||||
| Active site | 17 | 1 | Proton donor By similarity | ||||||
| Binding site | 19 | 1 | Substrate By similarity | ||||||
| Binding site | 48 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 66 | 1 | Substrate By similarity | ||||||
| Binding site | 68 | 1 | Substrate By similarity | ||||||
| Binding site | 83 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes." Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R. J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fusaro / DSM 804. |
| [2] | "Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis." Goenrich M., Thauer R.K., Yurimoto H., Kato N. Arch. Microbiol. 184:41-48(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, PATHWAY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000099 Genomic DNA. Translation: AAZ69907.1. |
| RefSeq | YP_304487.1. NC_007355.1. |
3D structure databases | |
| ProteinModelPortal | Q46DY5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 269797.Mbar_A0935. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAZ69907; AAZ69907; Mbar_A0935. |
| GeneID | 3627315. |
| KEGG | mba:Mbar_A0935. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1795. |
| HOGENOM | HOG000286408. |
| KO | K13812. |
| OMA | YNYGATK. |
| ProtClustDB | PRK13307. |
Enzyme and pathway databases | |
| BioCyc | MBAR269797:GHUW-952-MONOMER. |
| UniPathway | UPA00293. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. 3.30.230.60. 1 hit. |
| HAMAP | MF_01268. Fae_Hps. |
| InterPro | IPR013785. Aldolase_TIM. IPR020868. Bifunctional_enzyme_fae/hps. IPR014826. HCHO-activating_enzyme. IPR001754. OMPdeCOase_dom. IPR020568. Ribosomal_S5_D2-typ_fold. IPR011060. RibuloseP-bd_barrel. [Graphical view] |
| Pfam | PF08714. Fae. 1 hit. PF00215. OMPdecase. 1 hit. [Graphical view] |
| SMART | SM00934. OMPdecase. 1 hit. [Graphical view] |
| SUPFAM | SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF51366. RibP_bind_barrel. 1 hit. |
| TIGRFAMs | TIGR03126. one_C_fae. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | FAEHP_METBF | ||||||||
| Accession | Primary (citable) accession number: Q46DY5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
