Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase 1

Gene

FBA1

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

Pathway:iglycolysis

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Glyceraldehyde 3-phosphateBy similarity
Active sitei110 – 1101Proton donorBy similarity
Metal bindingi111 – 1111Zinc 1; catalyticBy similarity
Metal bindingi145 – 1451Zinc 2By similarity
Metal bindingi175 – 1751Zinc 2By similarity
Metal bindingi227 – 2271Zinc 1; catalyticBy similarity
Binding sitei228 – 2281Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi266 – 2661Zinc 1; catalyticBy similarity

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 1 (EC:4.1.2.13)
Short name:
FBP aldolase 1
Short name:
FBPA 1
Alternative name(s):
Fructose-1,6-bisphosphate aldolase 1
Gene namesi
Name:FBA1
ORF Names:PAAG_01995
OrganismiParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic identifieri502779 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides
ProteomesiUP000002059 Componenti: Partially assembled WGS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 360359Fructose-bisphosphate aldolase 1PRO_0000377379Add
BLAST

Expressioni

Inductioni

Preferentially expressed in yeast cells, the host parasitic phase.2 Publications

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi502779.XP_002796107.1.

Structurei

3D structure databases

ProteinModelPortaliQ96UH7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 2693Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

KOiK01624.
OrthoDBiEOG7HTHSN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
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.

Q96UH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVKDILSRK TGVIVGDDVL RLFQHAQEKV FAIPAINVTS SSTVVAALEA
60 70 80 90 100
ARDKNSPIIL QVSQGGAAFF AGKGVPNGKQ EASVAGAIAA AHYIRSIAPS
110 120 130 140 150
YGIPVVLHTD HCAKKLLPWL DGMLDADECY FKLHNEPLFS SHMIDLSEES
160 170 180 190 200
VEWNIETTAK YLKRAAPMKQ WLEMEIGITG GEEDGVNNES VDNNSLYTQP
210 220 230 240 250
EDIYTIYKTL SAISPYFSIA AGFGNVHGVY KPGNVRLHPE LLSKHQAYVK
260 270 280 290 300
EKTGSSKNKP VYLVFHGGSG STKAEFKEAI SYGVVKVNLD TDLQYAYLSG
310 320 330 340 350
VRDFVLKKKD YLMSAVGNPE GEDKPNKKYF DPRVWIREGE KTMSARVQEA
360
FDDFNTSNQL
Length:360
Mass (Da):39,632
Last modified:September 1, 2009 - v3
Checksum:i67475F644C58E162
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481Y → H in AAL25625 (PubMed:15588996).Curated
Sequence conflicti248 – 2481Y → H in AAL34519 (PubMed:15588996).Curated
Sequence conflicti344 – 3441S → C in AAL25625 (PubMed:15588996).Curated
Sequence conflicti344 – 3441S → C in AAL34519 (PubMed:15588996).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057387 Genomic DNA. Translation: AAL25625.2.
AY233454 mRNA. Translation: AAL34519.2.
KN293995 Genomic DNA. Translation: EEH39806.1.
RefSeqiXP_002796107.1. XM_002796061.1.

Genome annotation databases

GeneIDi9099250.
KEGGipbl:PAAG_01995.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057387 Genomic DNA. Translation: AAL25625.2.
AY233454 mRNA. Translation: AAL34519.2.
KN293995 Genomic DNA. Translation: EEH39806.1.
RefSeqiXP_002796107.1. XM_002796061.1.

3D structure databases

ProteinModelPortaliQ96UH7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi502779.XP_002796107.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9099250.
KEGGipbl:PAAG_01995.

Phylogenomic databases

KOiK01624.
OrthoDBiEOG7HTHSN.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Paracoccidioides brasiliensis presents two different cDNAs encoding homologues of the fructose 1,6-biphosphate aldolase: protein isolation, cloning of the cDNAs and genes, structural, phylogenetic, and expression analysis."
    Carneiro L.C., de Faria F.P., Felipe M.S.S., Pereira M., de Almeida Soares C.M.
    Fungal Genet. Biol. 42:51-60(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 328-339 AND 343-359, INDUCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-826 / Pb01.
  3. "Two-dimensional electrophoresis and characterization of antigens from Paracoccidioides brasiliensis."
    da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A., de Almeida Soares C.M.
    Microbes Infect. 3:535-542(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-37, INDUCTION.

Entry informationi

Entry nameiALF1_PARBA
AccessioniPrimary (citable) accession number: Q96UH7
Secondary accession number(s): C1GU00, Q8X219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: September 1, 2009
Last modified: June 24, 2015
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.