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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Streptomyces galbus
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.

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

pH dependencei

Optimum pH is 7.5.

Pathway: 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. no protein annotated in this organism
  3. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Glyceraldehyde 3-phosphateBy similarity
Active sitei95 – 951Proton donorBy similarity
Metal bindingi96 – 961Zinc 1; catalyticBy similarity
Metal bindingi131 – 1311Zinc 2By similarity
Metal bindingi161 – 1611Zinc 2By similarity
Metal bindingi212 – 2121Zinc 1; catalyticBy similarity
Binding sitei213 – 2131Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi249 – 2491Zinc 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 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
Synonyms:fda
OrganismiStreptomyces galbus
Taxonomic identifieri33898 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Fructose-bisphosphate aldolasePRO_0000178744Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9ZEM7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 2523Dihydroxyacetone phosphate bindingBy similarity
Regioni271 – 2744Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZEM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIATPEVYN EMLDRAKAGK FAYPAINVTS SQTLNAALRG FAEAESDGIV
60 70 80 90 100
QISTGGAEFL GGQYSKDMVT GAVALAEFAH IIAEKYPVNI ALHTDHCPKD
110 120 130 140 150
KLDGYVRPLL ALSKKRVEAG LGPLFQSHMW DGSAEPLADN LAIAQELLET
160 170 180 190 200
ARAAQIILEV EITPTGGEED GVSHEINDSL YTTVDDAIRT AEALGLGEKG
210 220 230 240 250
RYLLAASFGN VHGVYKPGNV VLRPELLKEL NEGVAARFGK ESPFDFVFHG
260 270 280 290 300
GSGSSEEEIR TALENGVVKM NLDTDTQYAF TRPVAGHMFA NYDGVLKVDG
310 320 330 340
EVGNKKAYDP RTWGKLAEAS MAARVVEATQ HLRSAGNKIK
Length:340
Mass (Da):36,550
Last modified:August 14, 2001 - v2
Checksum:i8DB47E14F8B8E9F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131707 Genomic DNA. Translation: CAA10483.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131707 Genomic DNA. Translation: CAA10483.2.

3D structure databases

ProteinModelPortaliQ9ZEM7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, nucleotide sequence and structural analysis of the Streptomyces galbus DSM40480 fda gene: the S. galbus fructose-1,6-bisphosphate aldolase is a member of the class II aldolases."
    Wehmeier U.F.
    FEMS Microbiol. Lett. 197:53-58(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 14077 / CBS 700.72 / DSM 40480 / NBRC 13399 / VKM Ac-160.

Entry informationi

Entry nameiALF_STRGB
AccessioniPrimary (citable) accession number: Q9ZEM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: June 24, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.