Fructose-bisphosphate aldolase - Helicobacter pylori

Names and origin

Protein names

Recommended 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
Ordered Locus Names:	HP_0176

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 By similarity.
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.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 307

307

Fructose-bisphosphate aldolase

PRO_0000178717

Regions

Region

211 – 213

3

Dihydroxyacetone phosphate binding By similarity

Region

253 – 256

4

Dihydroxyacetone phosphate binding By similarity

Sites

Active site

82

1

Proton donor By similarity

Metal binding

83

1

Zinc 1; catalytic By similarity

Metal binding

104

1

Zinc 2 By similarity

Metal binding

134

1

Zinc 2 By similarity

Metal binding

180

1

Zinc 1; catalytic By similarity

Metal binding

210

1

Zinc 1; catalytic By similarity

Binding site

49

1

Glyceraldehyde 3-phosphate By similarity

Binding site

181

1

Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

1

.

307

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P56109-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: ADC5696C67C69A45
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FASTA

307

33,773

        10         20         30         40         50         60 
MLVKGNEILL KAHKEGYGVG AFNFVNFEML NAIFEAGNEE NSPLFIQTSE GAIKYMGIDM 

        70         80         90        100        110        120 
AVGMVKTMCE RYPHIPVALH LDHGTTFESC EKAVKAGFTS VMIDASHHAF EENLELTSKV 

       130        140        150        160        170        180 
VKMAHNAGVS VEAELGRLMG IEDNISVDEK DAVLVNPKEA EQFVKESQVD YLAPAIGTSH 

       190        200        210        220        230        240 
GAFKFKGEPK LDFERLQEVK RLTNIPLVLH GASAIPDNVR KSYLDAGGDL KGSKGVPFEF 

       250        260        270        280        290        300 
LQESVKGGIN KVNTDTDLRI AFIAEVRKVA NEDKSQFDLR KFFSPAQLAL KNVVKERMKL 


LGSANKI

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References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J.

Venter J.C.
Nature 388:539-547(1997) [PubMed: 9252185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

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Cross-references

Sequence databases

AE000511 Genomic DNA. Translation: AAD07246.1.

PIR

H64541.

RefSeq

NP_206975.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3C4U	X-ray	1.83	A/B	1-307	[»]
3C52	X-ray	2.30	A/B	1-307	[»]
3C56	X-ray	2.30	A/B	1-307	[»]

ModBase

Search...

Genome annotation databases

GeneID

900140.

GenomeReviews

Gene locus HP_0176 in contig AE000511_GR.

KEGG

hpy:HP0176.

NMPDR

fig|85962.1.peg.173.

TIGR

HP_0176.

Phylogenomic databases

HOGENOM

P56109.

OMA

EWLKIIN

Enzyme and pathway databases

BRENDA

4.1.2.13. 1131.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01116. F_bP_aldolase. 1 hit.
[Graphical view]

PIRSF

PIRSF001359. F_bP_aldolase_II. 1 hit.

TIGRFAMs

TIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.

PROSITE

PS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

ALF_HELPY

Accession

Primary (citable) accession number: P56109

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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