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P58314 (ALF1_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name:fba
Ordered Locus Names:PF1956
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Activated by citrate.

Subunit structure

Homooctamer.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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 – 281281Fructose-bisphosphate aldolase class 1
PRO_0000138949

Sites

Active site1911Schiff-base intermediate with dihydroxyacetone-P

Experimental info

Mutagenesis1911K → A: Loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P58314 [UniParc].

Last modified October 18, 2001. Version 1.
Checksum: 19637AD0DA8CBD2F

FASTA28131,135
        10         20         30         40         50         60 
MEAPQNVGIK RRLKRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPRV IIRKVVRAGI 

        70         80         90        100        110        120 
DGVMMLPGLA RIAGDEVKPE VGLMIKLTSK TNLRPKPEQL LQSQLGFVDD AIKLGADAIA 

       130        140        150        160        170        180 
ATVYWGSPQE DVMMRQFAEI VSYAHDLGYP VVQFAYPRGP YIDEKYGKKE DYRVVMYGAR 

       190        200        210        220        230        240 
AAAESGADMI KTYWTGSKET FAKVVEAAAG VPVLLSGGAK TENPVDFLKV VWEVIEAGGA 

       250        260        270        280 
GAVVGRNIFQ RENPEPMIKA LIRVIHRNED PEEAAKAEGL I 

« 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], CHARACTERIZATION, MUTAGENESIS OF LYS-191.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF368256 Genomic DNA. Translation: AAK83936.1.
AE009950 Genomic DNA. Translation: AAL82080.1.
RefSeqNP_579685.1. NC_003413.1.

3D structure databases

ProteinModelPortalP58314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1956.

Proteomic databases

PRIDEP58314.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL82080; AAL82080; PF1956.
GeneID1469838.
KEGGpfu:PF1956.

Phylogenomic databases

eggNOGCOG1830.
HOGENOMHOG000224790.
KOK11645.
OMAATEGEYI.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11810.
SABIO-RKP58314.

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...

Entry information

Entry nameALF1_PYRFU
AccessionPrimary (citable) accession number: P58314
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: June 11, 2014
This is version 75 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