P0A4S2 (ALF_STRR6) 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:	spr0530

Organism

Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]

Taxonomic identifier

171101 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.
Post-translational modification	Phosphorylated. Ref.3
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference 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 – 293	293	Fructose-bisphosphate aldolase		PRO_0000178746
Regions
	Region	209 – 211	3	Dihydroxyacetone phosphate binding By similarity
	Region	230 – 233	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	85	1	Proton donor By similarity
	Metal binding	86	1	Zinc 1; catalytic By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	136	1	Zinc 2 By similarity
	Metal binding	178	1	Zinc 1; catalytic By similarity
	Metal binding	208	1	Zinc 1; catalytic By similarity
	Binding site	50	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	179	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A4S2 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 577D2A55713B6246	FASTA	293	31,402
	10 20 30 40 50 60 MAIVSAEKFV QAARDNGYAV GGFNTNNLEW TQAILRAAEA KKAPVLIQTS MGAAKYMGGY 70 80 90 100 110 120 KVARNLIANL VESMGITVPV AIHLDHGHYE DALECIEVGY TSIMFDGSHL PVEENLKLAK 130 140 150 160 170 180 EVVEKAHAKG ISVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP 190 200 210 220 230 240 YPVNWEGLDL DHLQKLTEAL PGFPIVLHGG SGIPDEQIQA AIKLGVAKVN VNTECQIAFA 250 260 270 280 290 NATRKFARDY EANEAEYDKK KLFDPRKFLA DGVKAIQASV EERIDVFGSE GKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and chromosomal location of a putative class-II aldolase gene from Streptococcus pneumoniae." Jado I., Fenoll A., Cepeda T., Casal J., Perez A. Curr. Microbiol. 39:31-36(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I. J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-255 / R6.
[3]	"Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates." Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A., Echenique J., Trombe M.C., Branny P. FEBS J. 272:1243-1254(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ005697 Genomic DNA. Translation: CAA06682.1. AE007317 Genomic DNA. Translation: AAK99334.1.
PIR	B97938.
RefSeq	NP_358124.1. NC_003098.1.
3D structure databases
ProteinModelPortal	P0A4S2.
ModBase	Search...
Protein-protein interaction databases
STRING	171101.spr0530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK99334; AAK99334; spr0530.
GeneID	933499.
KEGG	spr:spr0530.
PATRIC	19700919. VBIStrPne107296_0582.
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227793.
KO	K01624.
OMA	GMGECAD.
ProtClustDB	PRK07315.
Enzyme and pathway databases
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_STRR6

Accession

Primary (citable) accession number: P0A4S2
Secondary accession number(s): O65944

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program