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D1Z2Q4 (D1Z2Q4_METPS) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 25. Feed History...

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

Names and origin

Protein namesRecommended name:
Bifunctional enzyme Fae/Hps HAMAP-Rule MF_01268
Gene names
Name:fae EMBL BAI62976.1
Synonyms:fae-hps HAMAP-Rule MF_01268, hps EMBL BAI62976.1
Ordered Locus Names:MCP_2904 EMBL BAI62976.1
OrganismMethanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE) [Complete proteome] [HAMAP] EMBL BAI62976.1
Taxonomic identifier304371 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanocellalesMethanocellaceaeMethanocella

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H4MPT) to 5,10-methylenetetrahydromethanopterin By similarity. HAMAP-Rule MF_01268

Catalyzes the formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate By similarity. HAMAP-Rule MF_01268

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. HAMAP-Rule MF_01268

Sequence similarities

In the C-terminal section; belongs to the HPS/KGPDC family. HPS subfamily. HAMAP-Rule MF_01268

In the N-terminal section; belongs to the formaldehyde-activating enzyme family. HAMAP-Rule MF_01268

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region1 – 161161Formaldehyde-activating enzyme By similarity HAMAP-Rule MF_01268
Region162 – 3962353-hexulose-6-phosphate synthase By similarity HAMAP-Rule MF_01268

Sites

Active site171Proton donor By similarity HAMAP-Rule MF_01268
Binding site191Substrate By similarity HAMAP-Rule MF_01268
Binding site481Substrate; via carbonyl oxygen By similarity HAMAP-Rule MF_01268
Binding site661Substrate By similarity HAMAP-Rule MF_01268
Binding site681Substrate By similarity HAMAP-Rule MF_01268
Binding site831Substrate By similarity HAMAP-Rule MF_01268

Sequences

Sequence LengthMass (Da)Tools
D1Z2Q4 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 956B14C37D4C77E4

FASTA39642,680
        10         20         30         40         50         60 
MYLVGEALIG EGNEVAHIDL LVGDKAGPVG MAFANGMTNM SAGHTPLLAV VRPNLIPKPA 

        70         80         90        100        110        120 
TLIVPKVTVK NLEQAAQIFG PAQAAVAKAV ADAVEEGIIP KDQVESIVII VSVFVHPAAK 

       130        140        150        160        170        180 
DYTRIYKYNY GATRLALVRA MESFPPVDKV TFEKDRGTHA IMGYKIMRLW DPPYLQIAID 

       190        200        210        220        230        240 
APDLGVVERV LMQAPKNDHI IIEAGTPLIK RYGLEVISKI RAIKKDAFIV ADLKTLDTGN 

       250        260        270        280        290        300 
LEARMAADAT ADAVVCSGLA PLETIEKFCE EARKVGIYSI IDMLNVDNPA KVVEALKHKP 

       310        320        330        340        350        360 
DIVELHRGID TEGQKAEHAW GNIAGIKKAA GGKKLLVAVA GGVKVENVEV AMKGGADILV 

       370        380        390 
VGRAITNAKD IEGATRAFLR AMHKDEIDQY RIMTDF 

« Hide

References

[1]"Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella paludicola, the first cultivated representative of the order Methanocellales."
Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H., Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R., Mori K., Fujita N., Imachi H., Takai K.
PLoS ONE 6:E22898-E22898(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17711 / JCM 13418 / NBRC 101707 / SANAE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011532 Genomic DNA. Translation: BAI62976.1.
RefSeqYP_003357959.1. NC_013665.1.

3D structure databases

ProteinModelPortalD1Z2Q4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI62976; BAI62976; MCP_2904.
GeneID8682577.
KEGGmpd:MCP_2904.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000286408.
KOK13812.
OMAYNYGATK.

Enzyme and pathway databases

BioCycMPAL304371:GI7G-2965-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 nameD1Z2Q4_METPS
AccessionPrimary (citable) accession number: D1Z2Q4
Entry history
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: June 11, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)