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Protein

Fructose-bisphosphate aldolase

Gene

FBPA

Organism
Echinococcus multilocularis (Fox tapeworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

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. Glucose-6-phosphate isomerase (PGI)
  3. ATP-dependent 6-phosphofructokinase (EmuJ_001128600)
  4. Fructose-bisphosphate aldolase (EmuJ_000980100), Fructose-bisphosphate aldolase (EmuJ_000993800), Fructose-bisphosphate aldolase (EmuJ_000905600), Fructose-bisphosphate aldolase (EmuJ_000993700), Fructose-bisphosphate aldolase (FBPA)
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 sitei56 – 561SubstrateBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Gene namesi
Name:FBPA
OrganismiEchinococcus multilocularis (Fox tapeworm)
Taxonomic identifieri6211 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Fructose-bisphosphate aldolasePRO_0000216933Add
BLAST

Proteomic databases

PRIDEiQ9GP32.

Structurei

3D structure databases

ProteinModelPortaliQ9GP32.
SMRiQ9GP32. Positions 2-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GP32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFVPYLCA EKMKELRENA SAIVAPGKGL LAADESTNTI GKRFAAINLE
60 70 80 90 100
NTEENRRAYR ELLFTTDPEF AKHISGVILF HETVYQKTKD GKPFVELLRE
110 120 130 140 150
RGVLPGIKVD LGVVPLGGTA DECTTQGLDN LAQRCAQYYN DGCRFAKWRC
160 170 180 190 200
VLKISSHNPS YLAMLENANV LARYAFICQQ NGLVPIVEPE VLPDGDHDLE
210 220 230 240 250
TAQRVTEQVL SFVYKALADH HVYLEGTLLK PNMVTCGQSC TKKYSVEDNA
260 270 280 290 300
RATVEALQRT VPVAVPGVVF LSGGQSELDA TRNLNAINKY PGKKPWALSF
310 320 330 340 350
SFGRALQASA IAAWQGKPEN VKAGQAEFLQ LAKANGAASL GKFEGELKTA
360
AGQKSLFVAN HAY
Length:363
Mass (Da):39,727
Last modified:March 1, 2001 - v1
Checksum:i37862DEC55BA2B70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292376 mRNA. Translation: CAC18550.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292376 mRNA. Translation: CAC18550.1.

3D structure databases

ProteinModelPortaliQ9GP32.
SMRiQ9GP32. Positions 2-363.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9GP32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "mRNA trans-splicing in the human parasitic cestode Echinococcus multilocularis."
    Brehm K., Jensen K., Frosch M.
    J. Biol. Chem. 275:38311-38318(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: H-95.

Entry informationi

Entry nameiALF_ECHMU
AccessioniPrimary (citable) accession number: Q9GP32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.