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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
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 (pgi)
  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)DescriptionActionsGraphical viewLength
Binding sitei49Glyceraldehyde 3-phosphateBy similarity1
Active sitei82Proton donorBy similarity1
Metal bindingi83Zinc 1; catalyticBy similarity1
Metal bindingi104Zinc 2By similarity1
Metal bindingi134Zinc 2By similarity1
Metal bindingi180Zinc 1; catalyticBy similarity1
Binding sitei181Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi210Zinc 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

BRENDAi4.1.2.13. 2604.
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
Ordered Locus Names:HP_0176
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1287618.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787171 – 307Fructose-bisphosphate aldolaseAdd BLAST307

Proteomic databases

PaxDbiP56109.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi85962.HP0176.

Chemistry databases

BindingDBiP56109.

Structurei

Secondary structure

1307
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Beta strandi19 – 23Combined sources5
Helixi27 – 40Combined sources14
Beta strandi44 – 49Combined sources6
Helixi50 – 56Combined sources7
Helixi58 – 71Combined sources14
Beta strandi77 – 84Combined sources8
Helixi87 – 96Combined sources10
Beta strandi99 – 103Combined sources5
Helixi110 – 126Combined sources17
Beta strandi130 – 135Combined sources6
Helixi157 – 167Combined sources11
Beta strandi170 – 174Combined sources5
Helixi181 – 183Combined sources3
Beta strandi186 – 188Combined sources3
Helixi193 – 203Combined sources11
Beta strandi207 – 209Combined sources3
Helixi217 – 225Combined sources9
Helixi238 – 247Combined sources10
Beta strandi249 – 254Combined sources6
Helixi256 – 272Combined sources17
Helixi279 – 301Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C4UX-ray1.83A/B1-307[»]
3C52X-ray2.30A/B1-307[»]
3C56X-ray2.30A/B1-307[»]
ProteinModelPortaliP56109.
SMRiP56109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56109.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni211 – 213Dihydroxyacetone phosphate bindingBy similarity3
Regioni253 – 256Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D2N. Bacteria.
COG0191. LUCA.
KOiK01624.
OMAiVNTREMF.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR011289. Fruc_bis_ald_class-2.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVKGNEILL KAHKEGYGVG AFNFVNFEML NAIFEAGNEE NSPLFIQTSE
60 70 80 90 100
GAIKYMGIDM AVGMVKTMCE RYPHIPVALH LDHGTTFESC EKAVKAGFTS
110 120 130 140 150
VMIDASHHAF EENLELTSKV VKMAHNAGVS VEAELGRLMG IEDNISVDEK
160 170 180 190 200
DAVLVNPKEA EQFVKESQVD YLAPAIGTSH GAFKFKGEPK LDFERLQEVK
210 220 230 240 250
RLTNIPLVLH GASAIPDNVR KSYLDAGGDL KGSKGVPFEF LQESVKGGIN
260 270 280 290 300
KVNTDTDLRI AFIAEVRKVA NEDKSQFDLR KFFSPAQLAL KNVVKERMKL

LGSANKI
Length:307
Mass (Da):33,773
Last modified:November 1, 1997 - v1
Checksum:iADC5696C67C69A45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07246.1.
PIRiH64541.
RefSeqiNP_206975.1. NC_000915.1.
WP_000960471.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07246; AAD07246; HP_0176.
GeneIDi900140.
KEGGiheo:C694_00875.
hpy:HP0176.
PATRICi20591573. VBIHelPyl33062_0186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07246.1.
PIRiH64541.
RefSeqiNP_206975.1. NC_000915.1.
WP_000960471.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C4UX-ray1.83A/B1-307[»]
3C52X-ray2.30A/B1-307[»]
3C56X-ray2.30A/B1-307[»]
ProteinModelPortaliP56109.
SMRiP56109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi85962.HP0176.

Chemistry databases

BindingDBiP56109.
ChEMBLiCHEMBL1287618.

Proteomic databases

PaxDbiP56109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD07246; AAD07246; HP_0176.
GeneIDi900140.
KEGGiheo:C694_00875.
hpy:HP0176.
PATRICi20591573. VBIHelPyl33062_0186.

Phylogenomic databases

eggNOGiENOG4105D2N. Bacteria.
COG0191. LUCA.
KOiK01624.
OMAiVNTREMF.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BRENDAi4.1.2.13. 2604.

Miscellaneous databases

EvolutionaryTraceiP56109.
PROiP56109.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR011289. Fruc_bis_ald_class-2.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF_HELPY
AccessioniPrimary (citable) accession number: P56109
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 104 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.