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

fba

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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-1)
  3. ATP-dependent 6-phosphofructokinase (emp-3)
  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 sitei63Glyceraldehyde 3-phosphateBy similarity1
Active sitei112Proton donorBy similarity1
Metal bindingi113Zinc 1; catalyticBy similarity1
Metal bindingi147Zinc 2By similarity1
Metal bindingi177Zinc 2By similarity1
Metal bindingi229Zinc 1; catalyticBy similarity1
Binding sitei230Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi268Zinc 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 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
ORF Names:NCU07807
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 2, Linkage Group V

Organism-specific databases

EuPathDBiFungiDB:NCU07807.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787591 – 362Fructose-bisphosphate aldolaseAdd BLAST362

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP53444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 271Dihydroxyacetone phosphate bindingBy similarity3
Regioni290 – 293Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000227794.
InParanoidiP53444.
KOiK01624.
OMAiRMSKMGM.
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.

P53444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIFDELNLP AGVLYGDDVL KLFQYAREKQ FAIPACNVTS SSTAVAALEA
60 70 80 90 100
ARDQKAPIIL QTSQGGAAFF AGKGIKDSAE KREASVAGAI AAAHYIRSIA
110 120 130 140 150
PIYGIPVVLH TDHCAKKLLP WLDGMLEEDE KFFKANGVPL FSSHMIDLSE
160 170 180 190 200
EPVEENISTC VKYLKRMAPM KQWLEMEIGI TGGEEDGVDN SEVDNASLYT
210 220 230 240 250
QPEDIWQIEE AFRPISPYFS IAAGFGNVHG VYAPGNVKLH PELLGKHQAY
260 270 280 290 300
VSEKLGGKDK KPVFFVFHGG SGSSKEEYRE AISNGVVKVN VDTDLQWSYL
310 320 330 340 350
VGIRDYILNN IDYLRSQVGN PEGPNKPNKK KYDPRVWIRE GEKTMKARVE
360
EALKDFNAAG TV
Length:362
Mass (Da):39,889
Last modified:March 1, 2004 - v2
Checksum:iC402186EEEBD9368
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 15MGIFD…AGVLY → MRCPIPEHKQNLTFSLPL in AAB00930 (Ref. 1) CuratedAdd BLAST15
Sequence conflicti58 – 59II → SS in AAB00930 (Ref. 1) Curated2
Sequence conflicti66G → C in AAB00930 (Ref. 1) Curated1
Sequence conflicti82 – 84REA → ARD in AAB00930 (Ref. 1) Curated3
Sequence conflicti109L → RI in AAB00930 (Ref. 1) Curated1
Sequence conflicti120 – 126PWLDGML → FGDGIP in AAB00930 (Ref. 1) Curated7
Sequence conflicti211 – 212AF → DS in AAB00930 (Ref. 1) Curated2
Sequence conflicti222A → G in AAB00930 (Ref. 1) Curated1
Sequence conflicti242E → D in AAB00930 (Ref. 1) Curated1
Sequence conflicti247H → Q in AAB00930 (Ref. 1) Curated1
Sequence conflicti252S → P in AAB00930 (Ref. 1) Curated1
Sequence conflicti263V → F in AAB00930 (Ref. 1) Curated1
Sequence conflicti352 – 360ALKDFNAAG → GPQGPSNTTV in AAB00930 (Ref. 1) Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42380 Genomic DNA. Translation: AAB00930.1.
CM002240 Genomic DNA. Translation: ESA42348.1.
CM002240 Genomic DNA. Translation: ESA42349.1.
PIRiT47260.
RefSeqiXP_011394728.1. XM_011396426.1.
XP_011394729.1. XM_011396427.1.

Genome annotation databases

EnsemblFungiiESA42348; ESA42348; NCU07807.
ESA42349; ESA42349; NCU07807.
GeneIDi3874540.
KEGGincr:NCU07807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42380 Genomic DNA. Translation: AAB00930.1.
CM002240 Genomic DNA. Translation: ESA42348.1.
CM002240 Genomic DNA. Translation: ESA42349.1.
PIRiT47260.
RefSeqiXP_011394728.1. XM_011396426.1.
XP_011394729.1. XM_011396427.1.

3D structure databases

ProteinModelPortaliP53444.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiESA42348; ESA42348; NCU07807.
ESA42349; ESA42349; NCU07807.
GeneIDi3874540.
KEGGincr:NCU07807.

Organism-specific databases

EuPathDBiFungiDB:NCU07807.

Phylogenomic databases

HOGENOMiHOG000227794.
InParanoidiP53444.
KOiK01624.
OMAiRMSKMGM.
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_NEUCR
AccessioniPrimary (citable) accession number: P53444
Secondary accession number(s): A7UX41, Q7S1C1, V5IKX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 1, 2004
Last modified: November 30, 2016
This is version 121 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, Reference proteome

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.