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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase (pfkA), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp)
  4. Fructose-bisphosphate aldolase (fba)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56Glyceraldehyde 3-phosphateBy similarity1
Active sitei93Proton donorBy similarity1
Metal bindingi94Zinc 1; catalyticBy similarity1
Metal bindingi115Zinc 2By similarity1
Metal bindingi147Zinc 2By similarity1
Metal bindingi191Zinc 1; catalyticBy similarity1
Binding sitei192Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi234Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
Synonyms:fda
Ordered Locus Names:TP_0662
OrganismiTreponema pallidum (strain Nichols)
Taxonomic identifieri243276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
Proteomesi
  • UP000000811 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787531 – 332Fructose-bisphosphate aldolaseAdd BLAST332

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO83668, 4 interactors
STRINGi243276.TP0662

Structurei

3D structure databases

ProteinModelPortaliO83668
SMRiO83668
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni235 – 237Dihydroxyacetone phosphate bindingBy similarity3
Regioni277 – 280Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D2N Bacteria
COG0191 LUCA
KOiK01624
OMAiELCKDCI

Family and domain databases

CDDicd00947 TBP_aldolase_IIB, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000771 FBA_II
IPR011289 Fruc_bis_ald_class-2
PfamiView protein in Pfam
PF01116 F_bP_aldolase, 1 hit
PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
TIGRFAMsiTIGR00167 cbbA, 1 hit
TIGR01859 fruc_bis_ald_, 1 hit
PROSITEiView protein in PROSITE
PS00602 ALDOLASE_CLASS_II_1, 1 hit

Sequencei

Sequence statusi: Complete.

O83668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSYKALGLV NTKDLFAKAV KGGYAIPAYN FNNLEQLQAI IQACVETRSP
60 70 80 90 100
VILQVSSGAR KYANATLLRN MARGAVEYAH ELGVDIPIVL HLDHGDSLEL
110 120 130 140 150
CIDCIESGFS SVMIDGSALP YDENVALSRK VCEYAHARAD YVTVEGELGV
160 170 180 190 200
LAGVEDDVVA EKSHYTMPDE VEDFVKKTGV DSLAISIGTS HGRAKFTPEQ
210 220 230 240 250
CTRNADGVLI PPPLRFDILA EIEKRIPGFP IVLHGASSVP VEYVREVERY
260 270 280 290 300
GGNLPDSVGI PEEQLRKAAK SAVCKVNIDS DGRLAMTAAI RRVLTTKVDE
310 320 330
FDPRKYLGPA RDELKKLYMH KNKEVLGSAG RA
Length:332
Mass (Da):36,189
Last modified:November 1, 1998 - v1
Checksum:iB6D8D56BF99B52EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA Translation: AAC65635.1
PIRiG71297
RefSeqiWP_010882107.1, NC_021490.2

Genome annotation databases

EnsemblBacteriaiAAC65635; AAC65635; TP_0662
GeneIDi34331474
KEGGitpa:TP_0662

Similar proteinsi

Entry informationi

Entry nameiALF_TREPA
AccessioniPrimary (citable) accession number: O83668
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: November 22, 2017
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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