Q9ZMQ6 (ALF_HELPJ) Reviewed, UniProtKB/Swiss-Prot

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:	jhp_0162

Organism

Helicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	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-UniPathway
Molecular_function	fructose-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Fructose-bisphosphate aldolase		PRO_0000178718
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

Sequences

	Sequence		Length	Mass (Da)
	Q9ZMQ6 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 183D55744097E248	FASTA	307	33,798
	10 20 30 40 50 60 MLVKGNEILL KAHKEGYGVG AFNFVNFEML NAIFEAGNEE NSPLFIQASE GAIKYMGIDM 70 80 90 100 110 120 AVGMVKIMCE RYPHIPVALH LDHGTTFESC EKAVKAGFTS VMIDASHHAF EENLELTSKV 130 140 150 160 170 180 VKMAHNAGVS VEAELGRLMG IEDNISVDEK DAVLVNPKEA ERFVKESQVD YLAPAIGTSH 190 200 210 220 230 240 GAFKFKGEPK LDFERLQEVK RLTNIPLVLH GASAIPDDVR KSYLDAGGDL KGSKGVPFEF 250 260 270 280 290 300 LQESIKGGIN KVNTDTDLRI AFIAEVRKVA NEDKSQFDLR KFFSPAQLAL KNVVKERMKL LGSANKI

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J99.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001439 Genomic DNA. Translation: AAD05734.1.
PIR	C71967.
RefSeq	NP_222883.1. NC_000921.1.
3D structure databases
ProteinModelPortal	Q9ZMQ6.
ModBase	Search...
Protein-protein interaction databases
STRING	85963.jhp0162.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD05734; AAD05734; jhp_0162.
GeneID	889011.
KEGG	hpj:jhp0162.
PATRIC	20604944. VBIHelPyl98156_0184.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
KO	K01624.
OMA	AIKETVI.
ProtClustDB	PRK05835.
Enzyme and pathway databases
BioCyc	HPYL85963:GJB9-169-MONOMER.
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR011289. Fruc_bis_ald_class-2. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
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...

Entry information

Entry name

ALF_HELPJ

Accession

Primary (citable) accession number: Q9ZMQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program