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Protein

Fructose-bisphosphate aldolase 2

Gene

FBA2

Organism
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 (PAAG_06526)
  3. ATP-dependent 6-phosphofructokinase (PAAG_01583)
  4. Fructose-bisphosphate aldolase 1 (FBA1), Fructose-bisphosphate aldolase 2 (FBA2)
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 sitei61Glyceraldehyde 3-phosphateBy similarity1
Active sitei109Proton donorBy similarity1
Metal bindingi110Zinc 1; catalyticBy similarity1
Metal bindingi144Zinc 2By similarity1
Metal bindingi174Zinc 2By similarity1
Metal bindingi226Zinc 1; catalyticBy similarity1
Binding sitei227Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi264Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 2 (EC:4.1.2.13)
Short name:
FBP aldolase 2
Short name:
FBPA 2
Alternative name(s):
Fructose-1,6-bisphosphate aldolase 2
Gene namesi
Name:FBA2
OrganismiParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifieri502779 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisParacoccidioides

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001787602 – 363Fructose-bisphosphate aldolase 2Add BLAST362

Expressioni

Inductioni

Only detected in the mycelia phase, but not in yeast cells.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8J0N6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni265 – 267Dihydroxyacetone phosphate bindingBy similarity3

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR006411. Fruct_bisP_bact.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 2 hits.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8J0N6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVKDLLSRK TGVIVGDDVL RLFQHAQENV FAIPAIMVTS SSTGSALEAA
60 70 80 90 100
RDKSPIVLQT SNGAAYFAGK GKGVSNDGQS VAGSIAIAAA HYIRSQAPAY
110 120 130 140 150
GIPVVLHTDH CAKKLLPWLD GMLDADECYS KLHNEPLFSS HMIDLSEESV
160 170 180 190 200
EWNIETTAKY LKRAAPMKQW LEMEIGITGG EEDGVNNESV DNNSLYTQPE
210 220 230 240 250
DIYTIYKTLS AISPYFSIAA GFGNVHGVYR GDIALRPLLR HLHNAKYDEQ
260 270 280 290 300
LKCLQDPLGF FVFHGGSGSS HQPATSITSE FAAKGRVDLE KVAYLPGTSS
310 320 330 340 350
LVIAPKDYLM SPYGIPVVLH TDHCKYFDPR VQIREGLKHM SARVQEAKDD
360
FNDSNQAKKL LPW
Length:363
Mass (Da):39,770
Last modified:October 1, 2003 - v2
Checksum:i929C731386F46D76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY172327 mRNA. Translation: AAN85569.2.
AY581212 Genomic DNA. Translation: AAS99115.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY172327 mRNA. Translation: AAN85569.2.
AY581212 Genomic DNA. Translation: AAS99115.2.

3D structure databases

ProteinModelPortaliQ8J0N6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR006411. Fruct_bisP_bact.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 2 hits.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF2_PARBA
AccessioniPrimary (citable) accession number: Q8J0N6
Secondary accession number(s): Q6PT81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

The DNA coding for this protein is not found in the complete genome of strain ATCC MYA-826 / Pb01.Curated

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.