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

Putative fructose-bisphosphate aldolase

Gene

CIMG_05755

Organism
Coccidioides immitis (strain RS) (Valley fever fungus)
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

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 (CIMG_07844)
  3. ATP-dependent 6-phosphofructokinase (CIMG_08879)
  4. Putative fructose-bisphosphate aldolase (CIMG_05755)
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
Active sitei86Proton donorBy similarity1
Metal bindingi87Zinc 1; catalyticBy similarity1
Metal bindingi116Zinc 2By similarity1
Metal bindingi146Zinc 2By similarity1
Metal bindingi192Zinc 1; catalyticBy similarity1
Binding sitei193Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi223Zinc 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:
Putative fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Putative fructose-1,6-bisphosphate aldolase
Gene namesi
ORF Names:CIMG_05755
OrganismiCoccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic identifieri246410 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenales incertae sedisCoccidioides
Proteomesi
  • UP000001261 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:CIMG_05755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004037871 – 302Putative fructose-bisphosphate aldolaseAdd BLAST302

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi246410.XP_001241859.1.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 20Combined sources9
Beta strandi25 – 29Combined sources5
Helixi33 – 45Combined sources13
Beta strandi50 – 54Combined sources5
Helixi56 – 62Combined sources7
Helixi65 – 76Combined sources12
Beta strandi81 – 88Combined sources8
Helixi91 – 99Combined sources9
Beta strandi111 – 115Combined sources5
Helixi122 – 137Combined sources16
Turni138 – 140Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi147 – 149Combined sources3
Helixi170 – 177Combined sources8
Turni178 – 180Combined sources3
Beta strandi182 – 184Combined sources3
Helixi204 – 214Combined sources11
Turni215 – 217Combined sources3
Beta strandi218 – 222Combined sources5
Helixi230 – 238Combined sources9
Beta strandi241 – 247Combined sources7
Helixi248 – 261Combined sources14
Turni262 – 264Combined sources3
Helixi267 – 288Combined sources22
Helixi294 – 297Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PM6X-ray2.20A/B1-302[»]
ProteinModelPortaliP0CJ44.
SMRiP0CJ44.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CJ44.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni224 – 226Dihydroxyacetone phosphate bindingBy similarity3
Regioni245 – 248Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IKER. Eukaryota.
KOG4153. Eukaryota.
COG0191. LUCA.
ENOG4111ZYV. LUCA.
InParanoidiP0CJ44.
KOiK01624.
OrthoDBiEOG092C3TYK.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.

Sequencei

Sequence statusi: Complete.

P0CJ44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHPSLKSNR ALPLLTFART HSFAIPAICV YNLEGILAII RAAEHKRSPA
60 70 80 90 100
MILLFPWAIQ YADSLLVRTA ASACRAASVP ITLHLDHAQD PEIIKRAADL
110 120 130 140 150
SRSETHEPGF DSIMVDMSHF SKEENLRLTR ELVAYCNARG IATEAEPGRI
160 170 180 190 200
EGGEDGVQDT VDLEGVLTTP EESEEFVATG INWLAPAFGN VHGNYGPRGV
210 220 230 240 250
QLDYERLQRI NEAVGERVGL VLHGADPFTK EIFEKCIERG VAKVNVNRAV
260 270 280 290 300
NNEYVKVMRE KAGSLPITRL HEEVTNAMQA AVEKIMDMID STGKAEFMMD

EK
Length:302
Mass (Da):33,389
Last modified:January 11, 2011 - v1
Checksum:i3FBF318A0A3421C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704912 Genomic DNA. Translation: EAS30276.3.
RefSeqiXP_001241859.1. XM_001241858.2.

Genome annotation databases

EnsemblFungiiEAS30276; EAS30276; CIMG_05755.
GeneIDi4561677.
KEGGicim:CIMG_05755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704912 Genomic DNA. Translation: EAS30276.3.
RefSeqiXP_001241859.1. XM_001241858.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PM6X-ray2.20A/B1-302[»]
ProteinModelPortaliP0CJ44.
SMRiP0CJ44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246410.XP_001241859.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAS30276; EAS30276; CIMG_05755.
GeneIDi4561677.
KEGGicim:CIMG_05755.

Organism-specific databases

EuPathDBiFungiDB:CIMG_05755.

Phylogenomic databases

eggNOGiENOG410IKER. Eukaryota.
KOG4153. Eukaryota.
COG0191. LUCA.
ENOG4111ZYV. LUCA.
InParanoidiP0CJ44.
KOiK01624.
OrthoDBiEOG092C3TYK.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Miscellaneous databases

EvolutionaryTraceiP0CJ44.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALF_COCIM
AccessioniPrimary (citable) accession number: P0CJ44
Secondary accession number(s): J3K6Q1, J3K765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.