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

Gene

FBA1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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

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 (PGI1)
  3. ATP-dependent 6-phosphofructokinase (PFK2), ATP-dependent 6-phosphofructokinase (PFK1)
  4. Fructose-bisphosphate aldolase (FBA1)
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 sitei62Glyceraldehyde 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 bindingi265Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • glycolytic process Source: UniProtKB-UniPathway
  • induction by symbiont of host defense response Source: CGD
  • interaction with host Source: CGD
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 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
37 kDa major allergen
Fructose-1,6-bisphosphate aldolase
IgE-binding allergen
Gene namesi
Name:FBA1
ORF Names:CaO19.12088, CaO19.4618
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000186998. FBA1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cell surface Source: CGD
  • cytoplasm Source: UniProtKB-SubCell
  • fungal-type cell wall Source: CGD
  • hyphal cell wall Source: CGD
  • plasma membrane Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei5990. Cand a FPA.

Chemistry databases

ChEMBLiCHEMBL1287619.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001787572 – 359Fructose-bisphosphate aldolaseAdd BLAST358

Proteomic databases

PRIDEiQ9URB4.

2D gel databases

COMPLUYEAST-2DPAGEQ9URB4.

Interactioni

Subunit structurei

Homodimer.By similarity

Chemistry databases

BindingDBiQ9URB4.

Structurei

3D structure databases

ProteinModelPortaliQ9URB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni266 – 268Dihydroxyacetone phosphate bindingBy similarity3
Regioni287 – 290Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

InParanoidiQ9URB4.
KOiK01624.
OrthoDBiEOG092C385G.

Family and domain databases

CDDicd00946. FBP_aldolase_IIA. 1 hit.
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]
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.

Q9URB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPAVLSKS GVIYGKDVKD LFDYAQEKGF AIPAINVTSS STVVAALEAA
60 70 80 90 100
RDNKAPIILQ TSQGGAAYFA GKGVDNKDQA ASIAGSIAAA HYIRAIAPTY
110 120 130 140 150
GIPVVLHTDH CAKKLLPWFD GMLKADEEFF AKTGTPLFSS HMLDLSEETD
160 170 180 190 200
DENIATCAKY FERMAKMGQW LEMEIGITGG EEDGVNNEHV EKDALYTSPE
210 220 230 240 250
TVFAVYESLH KISPNFSIAA AFGNVHGVYK PGNVQLRPEI LGDHQVYAKK
260 270 280 290 300
QIGTDAKHPL YLVFHGGSGS TQEEFNTAIK NGVVKVNLDT DCQYAYLTGI
310 320 330 340 350
RDYVTNKIEY LKAPVGNPEG ADKPNKKYFD PRVWVREGEK TMSKRIAEAL

DIFHTKGQL
Length:359
Mass (Da):39,215
Last modified:March 3, 2009 - v2
Checksum:i030943199E4D6C28
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16K → L AA sequence (PubMed:1548078).Curated1
Sequence conflicti39 – 41SSS → WSW AA sequence (PubMed:1548078).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000005 Genomic DNA. Translation: EAL04108.1.
AACQ01000006 Genomic DNA. Translation: EAL03953.1.
PIRiA43853.
RefSeqiXP_722690.1. XM_717597.1.
XP_722836.1. XM_717743.1.

Genome annotation databases

EnsemblFungiiEAL03953; EAL03953; CaO19.4618.
EAL04108; EAL04108; CaO19.12088.
GeneIDi3635548.
3635585.
KEGGical:CaO19.12088.
cal:CaO19.4618.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000005 Genomic DNA. Translation: EAL04108.1.
AACQ01000006 Genomic DNA. Translation: EAL03953.1.
PIRiA43853.
RefSeqiXP_722690.1. XM_717597.1.
XP_722836.1. XM_717743.1.

3D structure databases

ProteinModelPortaliQ9URB4.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ9URB4.
ChEMBLiCHEMBL1287619.

Protein family/group databases

Allergomei5990. Cand a FPA.

2D gel databases

COMPLUYEAST-2DPAGEQ9URB4.

Proteomic databases

PRIDEiQ9URB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL03953; EAL03953; CaO19.4618.
EAL04108; EAL04108; CaO19.12088.
GeneIDi3635548.
3635585.
KEGGical:CaO19.12088.
cal:CaO19.4618.

Organism-specific databases

CGDiCAL0000186998. FBA1.

Phylogenomic databases

InParanoidiQ9URB4.
KOiK01624.
OrthoDBiEOG092C385G.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

CDDicd00946. FBP_aldolase_IIA. 1 hit.
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]
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...

Entry informationi

Entry nameiALF_CANAL
AccessioniPrimary (citable) accession number: Q9URB4
Secondary accession number(s): Q5AMM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 3, 2009
Last modified: November 30, 2016
This is version 95 of the entry and version 2 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. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.