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O83668 (ALF_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Synonyms:fda
Ordered Locus Names:TP_0662
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfructose 1,6-bisphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Fructose-bisphosphate aldolase
PRO_0000178753

Regions

Region235 – 2373Dihydroxyacetone phosphate binding By similarity
Region277 – 2804Dihydroxyacetone phosphate binding By similarity

Sites

Active site931Proton donor By similarity
Metal binding941Zinc 1; catalytic By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1471Zinc 2 By similarity
Metal binding1911Zinc 1; catalytic By similarity
Metal binding2341Zinc 1; catalytic By similarity
Binding site561Glyceraldehyde 3-phosphate By similarity
Binding site1921Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O83668 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: B6D8D56BF99B52EA

FASTA33236,189
        10         20         30         40         50         60 
MTSYKALGLV NTKDLFAKAV KGGYAIPAYN FNNLEQLQAI IQACVETRSP VILQVSSGAR 

        70         80         90        100        110        120 
KYANATLLRN MARGAVEYAH ELGVDIPIVL HLDHGDSLEL CIDCIESGFS SVMIDGSALP 

       130        140        150        160        170        180 
YDENVALSRK VCEYAHARAD YVTVEGELGV LAGVEDDVVA EKSHYTMPDE VEDFVKKTGV 

       190        200        210        220        230        240 
DSLAISIGTS HGRAKFTPEQ CTRNADGVLI PPPLRFDILA EIEKRIPGFP IVLHGASSVP 

       250        260        270        280        290        300 
VEYVREVERY GGNLPDSVGI PEEQLRKAAK SAVCKVNIDS DGRLAMTAAI RRVLTTKVDE 

       310        320        330 
FDPRKYLGPA RDELKKLYMH KNKEVLGSAG RA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000520 Genomic DNA. Translation: AAC65635.1.
PIRG71297.
RefSeqNP_219099.1. NC_000919.1.
YP_008091495.1. NC_021490.2.

3D structure databases

ProteinModelPortalO83668.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO83668. 4 interactions.
STRING243276.TP0662.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65635; AAC65635; TP_0662.
GeneID15851952.
2611197.
KEGGtpa:TP0662.
tpw:TPANIC_0662.
PATRIC20531397. VBITrePal57110_0703.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAELCKDCI.
OrthoDBEOG6HXJ7B.
ProtClustDBPRK07084.

Enzyme and pathway databases

BioCycTPAL243276:GC1H-703-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_TREPA
AccessionPrimary (citable) accession number: O83668
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 89 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