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P58315 (ALF1_THETK) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 57. 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:
Fructose-bisphosphate aldolase class 1

EC=4.1.2.13
Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name=FBP aldolase
Short name=FBPA
Gene names
Name:fba
Ordered Locus Names:TTX_1278
OrganismThermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1) [Complete proteome] [HAMAP]
Taxonomic identifier768679 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.1

Enzyme regulation

Activated by citrate. Ref.1

Subunit structure

Homodecamer (dimer of pentamers). Ref.1 Ref.3 Ref.4

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Fructose-bisphosphate aldolase class 1
PRO_0000138952

Regions

Region24 – 252Substrate binding
Region177 – 1793Substrate binding
Region202 – 2043Substrate binding
Region231 – 2322Substrate binding

Sites

Active site1461Proton donor
Active site1771Schiff-base intermediate with dihydroxyacetone-P
Binding site291Substrate
Binding site331Substrate
Binding site1441Substrate
Binding site1481Substrate

Experimental info

Mutagenesis1441W → E: Loss of FBP aldolase activity; when associated with F-146. Ref.4
Mutagenesis1461Y → F: The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144. Ref.4

Secondary structure

............................................... 263
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58315 [UniParc].

Last modified October 18, 2001. Version 1.
Checksum: 1399A6D0CF4F0D9E

FASTA26328,705
        10         20         30         40         50         60 
MANLTEKFLR IFARRGKSII LAYDHGIEHG PADFMDNPDS ADPEYILRLA RDAGFDGVVF 

        70         80         90        100        110        120 
QRGIAEKYYD GSVPLILKLN GKTTLYNGEP VSVANCSVEE AVSLGASAVG YTIYPGSGFE 

       130        140        150        160        170        180 
WKMFEELARI KRDAVKFDLP LVVWSYPRGG KVVNETAPEI VAYAARIALE LGADAMKIKY 

       190        200        210        220        230        240 
TGDPKTFSWA VKVAGKVPVL MSGGPKTKTE EDFLKQVEGV LEAGALGIAV GRNVWQRRDA 

       250        260 
LKFARALAEL VYGGKKLAEP LNV 

« Hide

References

« Hide 'large scale' references
[1]"Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolases."
Siebers B., Brinkmann H., Doerr C., Tjaden B., Lilie H., van der Oost J., Verhees C.H.
J. Biol. Chem. 276:28710-28718(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
[2]"The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota."
Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D., Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M., Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C., Hensel R.
PLoS ONE 6:E24222-E24222(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
[3]"Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins."
Lorentzen E., Pohl E., Zwart P., Stark A., Russell R.B., Knura T., Hensel R., Siebers B.
J. Biol. Chem. 278:47253-47260(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
[4]"Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates."
Lorentzen E., Siebers B., Hensel R., Pohl E.
Biochemistry 44:4222-4229(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLU-144 AND PHE-146 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF TRP-144 AND TYR-146, REACTION MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ310483 Genomic DNA. Translation: CAC48235.1.
FN869859 Genomic DNA. Translation: CCC81912.1.
RefSeqYP_004892990.1. NC_016070.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJXX-ray1.90A/B/C/D/E/F/G/H/I/J1-263[»]
1OK4X-ray2.10A/B/C/D/E/F/G/H/I/J1-263[»]
1OK6X-ray2.40A/B/C/D/E/F/G/H/I/J1-263[»]
1W8SX-ray1.85A/B/C/D/E/F/G/H/I/J1-263[»]
2YCEX-ray1.93A/B/C/D/E/F/G/H/I/J1-263[»]
ProteinModelPortalP58315.
SMRP58315. Positions 2-255.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC81912; CCC81912; TTX_1278.
GeneID11262157.
KEGGttn:TTX_1278.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK11645.
OMAYDHGIEH.

Enzyme and pathway databases

BioCycTTEN768679:GJSY-1253-MONOMER.
SABIO-RKP58315.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFPIRSF038992. Aldolase_Ia. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP58315.

Entry information

Entry nameALF1_THETK
AccessionPrimary (citable) accession number: P58315
Secondary accession number(s): G4RK17
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: October 16, 2013
This is version 57 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references