Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q46DY5 (FAEHP_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional enzyme Fae/Hps

Including the following 2 domains:

  1. Formaldehyde-activating enzyme
    Short name=Fae
    EC=4.3.3.-
  2. 3-hexulose-6-phosphate synthase
    Short name=HPS
    EC=4.1.2.43
    Alternative name(s):
    D-arabino-3-hexulose-6-phosphate formaldehyde lyase
Gene names
Name:faeB-hpsB
Ordered Locus Names:Mbar_A0935
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Bifunctional enzyme Fae/Hps HAMAP-Rule MF_01268
PRO_0000235168

Regions

Region1 – 161161Formaldehyde-activating enzyme HAMAP-Rule MF_01268
Region162 – 3922313-hexulose-6-phosphate synthase HAMAP-Rule MF_01268

Sites

Active site171Proton donor By similarity
Binding site191Substrate By similarity
Binding site481Substrate; via carbonyl oxygen By similarity
Binding site661Substrate By similarity
Binding site681Substrate By similarity
Binding site831Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46DY5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: AE132C4FBBAC00A1

FASTA39242,415
        10         20         30         40         50         60 
MFQIGEALMG QGAELAHVDL MIGDKGGPVG QAFANGLTQL SVGHTPLLSV IRPNLPPKPS 

        70         80         90        100        110        120 
TLIIPKVTVK NMEQAGKIFG PAQAAVAKAV ADSVEEGVIS KDQVEEIVIV ASVFIHPDAQ 

       130        140        150        160        170        180 
DYNKIYRYNY GATKLAIKRA LGGFPDINTV LEESNKSTHA IMGFKVTRLW DPPYLQVAFD 

       190        200        210        220        230        240 
NPDIEFVQSA ISQIPKSDHV IIEAGTPLIK RYGMDVISRI REVRPDAFIV ADLKTLDTGN 

       250        260        270        280        290        300 
LEARMVADAA GDAIVVSALA PISTIDKLIE EAHKTGIYAV MDTLNQQDPI SVLKQLKVMP 

       310        320        330        340        350        360 
DVIELHRGID IEATEHAWGN IAEIKKIAPK ILVAVAGGVR LDKVPVALGQ GADILVVGRA 

       370        380        390 
ITNSKDVREV AEQFINSLNK PEIDQFRVMT DF 

« Hide

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.
RefSeqYP_304487.1. NC_007355.1.

3D structure databases

ProteinModelPortalQ46DY5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269797.Mbar_A0935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ69907; AAZ69907; Mbar_A0935.
GeneID3627315.
KEGGmba:Mbar_A0935.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1795.
HOGENOMHOG000286408.
KOK13812.
OMAYNYGATK.
ProtClustDBPRK13307.

Enzyme and pathway databases

BioCycMBAR269797:GHUW-952-MONOMER.
UniPathwayUPA00293.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.30.230.60. 1 hit.
HAMAPMF_01268. Fae_Hps.
InterProIPR013785. 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]
PfamPF08714. Fae. 1 hit.
PF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
SSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR03126. one_C_fae. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFAEHP_METBF
AccessionPrimary (citable) accession number: Q46DY5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways