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Protein

Fructose-bisphosphate aldolase

Gene

fda

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
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.By similarity

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.By similarity
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)
  3. ATP-dependent 6-phosphofructokinase 1 (pfkA1), ATP-dependent 6-phosphofructokinase 2 (pfkA2)
  4. Fructose-bisphosphate aldolase (fda)
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 sitei50 – 501Glyceraldehyde 3-phosphateBy similarity
Active sitei83 – 831Proton donorBy similarity
Metal bindingi84 – 841Zinc 1; catalyticBy similarity
Metal bindingi105 – 1051Zinc 2By similarity
Metal bindingi142 – 1421Zinc 2By similarity
Metal bindingi198 – 1981Zinc 1; catalyticBy similarity
Binding sitei199 – 1991Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi232 – 2321Zinc 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 aldolaseBy similarity (EC:4.1.2.13)
Short name:
FBP aldolaseBy similarity
Short name:
FBPABy similarity
Alternative name(s):
Fructose-1,6-bisphosphate aldolaseBy similarity
Gene namesi
Name:fdaImported
Ordered Locus Names:all4563
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 359358Fructose-bisphosphate aldolaseBy similarityPRO_0000366199Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi103690.all4563.

Structurei

3D structure databases

ProteinModelPortaliQ8YNK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni233 – 2353Dihydroxyacetone phosphate bindingBy similarity
Regioni275 – 2784Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the class II fructose-bisphosphate aldolase family.Sequence Analysis

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiDRYQQFW.
OrthoDBiEOG6HXJ7B.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 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.

Q8YNK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVPLRLLL DHAAENGYGI PAFNVNNLEQ IQAILKAAAE TDSPVILQAS
60 70 80 90 100
RGARNYAGEN FLRHLILAAV ETYPEIPIVM HQDHGNAPST CYSAIKNNFT
110 120 130 140 150
SVMMDGSLEA DAKTPASFEY NVNVTREVVN VAHALGVSVE GELGCLGSLE
160 170 180 190 200
TGAGEAEDGH GFEGTLDHSQ LLTDPDEAVN FVEATQVDAL AVAIGTSHGA
210 220 230 240 250
YKFTRKPTGE ILAISRIEEI HRRLPNTHLV MHGSSSVPED LIALINEYGG
260 270 280 290 300
AIPETYGVPV EEIQKGIKSG VRKVNIDTDN RLAITAAVRE ALAKNPKEFD
310 320 330 340 350
PRHFLKPSIT YMQKVCAERY VQFGTAGNAS KIKQVSLETF AAKYAKGELN

AISKAAAKV
Length:359
Mass (Da):38,617
Last modified:March 1, 2002 - v1
Checksum:iE91D84D7591007B1
GO

Mass spectrometryi

Molecular mass is 38764±1 Da from positions 1 - 359. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB76262.1.
PIRiAC2376.
RefSeqiWP_010998695.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB76262; BAB76262; BAB76262.
KEGGiana:all4563.
PATRICi22779738. VBINosSp37423_5315.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB76262.1.
PIRiAC2376.
RefSeqiWP_010998695.1. NC_003272.1.

3D structure databases

ProteinModelPortaliQ8YNK2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi103690.all4563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB76262; BAB76262; BAB76262.
KEGGiana:all4563.
PATRICi22779738. VBINosSp37423_5315.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiDRYQQFW.
OrthoDBiEOG6HXJ7B.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.
  2. Singh H., Rajaram H., Apte S.K.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 282-289, MASS SPECTROMETRY.

Entry informationi

Entry nameiALF_NOSS1
AccessioniPrimary (citable) accession number: Q8YNK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 1, 2002
Last modified: July 22, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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.