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Q9ZEM7 (ALF_STRGB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Synonyms:fda
OrganismStreptomyces galbus
Taxonomic identifier33898 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Fructose-bisphosphate aldolase
PRO_0000178744

Regions

Region250 – 2523Dihydroxyacetone phosphate binding By similarity
Region271 – 2744Dihydroxyacetone phosphate binding By similarity

Sites

Active site951Proton donor By similarity
Metal binding961Zinc 1; catalytic By similarity
Metal binding1311Zinc 2 By similarity
Metal binding1611Zinc 2 By similarity
Metal binding2121Zinc 1; catalytic By similarity
Metal binding2491Zinc 1; catalytic By similarity
Binding site531Glyceraldehyde 3-phosphate By similarity
Binding site2131Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZEM7 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 8DB47E14F8B8E9F7

FASTA34036,550
        10         20         30         40         50         60 
MPIATPEVYN EMLDRAKAGK FAYPAINVTS SQTLNAALRG FAEAESDGIV QISTGGAEFL 

        70         80         90        100        110        120 
GGQYSKDMVT GAVALAEFAH IIAEKYPVNI ALHTDHCPKD KLDGYVRPLL ALSKKRVEAG 

       130        140        150        160        170        180 
LGPLFQSHMW DGSAEPLADN LAIAQELLET ARAAQIILEV EITPTGGEED GVSHEINDSL 

       190        200        210        220        230        240 
YTTVDDAIRT AEALGLGEKG RYLLAASFGN VHGVYKPGNV VLRPELLKEL NEGVAARFGK 

       250        260        270        280        290        300 
ESPFDFVFHG GSGSSEEEIR TALENGVVKM NLDTDTQYAF TRPVAGHMFA NYDGVLKVDG 

       310        320        330        340 
EVGNKKAYDP RTWGKLAEAS MAARVVEATQ HLRSAGNKIK

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ131707 Genomic DNA. Translation: CAA10483.2.

3D structure databases

ProteinModelPortalQ9ZEM7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_STRGB
AccessionPrimary (citable) accession number: Q9ZEM7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: April 3, 2013
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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