Q9I5Y1 (ALF_PSEAE) 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
Synonyms:	fda
Ordered Locus Names:	PA0555

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	354 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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	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 – 354	354	Fructose-bisphosphate aldolase		PRO_0000178725
Regions
	Region	233 – 235	3	Dihydroxyacetone phosphate binding By similarity
	Region	275 – 278	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	83	1	Proton donor By similarity
	Metal binding	84	1	Zinc 1; catalytic By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	142	1	Zinc 2 By similarity
	Metal binding	198	1	Zinc 1; catalytic By similarity
	Metal binding	232	1	Zinc 1; catalytic By similarity
	Binding site	50	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	199	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9I5Y1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 08864F52A39FC9C7	FASTA	354	38,574
	10 20 30 40 50 60 MALISMRQML DHAAEFGYGV PAFNVNNLEQ MRAIMEAADK TDSPVIVQAS AGARKYAGAP 70 80 90 100 110 120 FLRHLILAAI EEFPHIPVVM HQDHGTSPDV CQRSIQLGFS SVMMDGSLRE DGKTPADYDY 130 140 150 160 170 180 NVRVTQQTVA FAHACGVSVE GELGCLGSLE TGMAGEEDGV GAEGVLDHSQ LLTDPEEAAD 190 200 210 220 230 240 FVKKTKVDAL AIAIGTSHGA YKFTKPPTGD TLSIQRIKEI HARIPDTHLV MHGSSSVPQD 250 260 270 280 290 300 WLAIINEYGG EIKETYGVPV EEIVEGIKYG VRKVNIDTDL RLASTGAIRR FLAQNPSEFD 310 320 330 340 350 PRKYFSKTVE AMRDICIARY EAFGTAGNAS KIKPISLEGM FQRYARGELD PKVN

References

[1]

"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004091 Genomic DNA. Translation: AAG03944.1.
PIR	C83575.
RefSeq	NP_249246.1. NC_002516.2.
3D structure databases
ProteinModelPortal	Q9I5Y1.
SMR	Q9I5Y1. Positions 3-338.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA0555.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	880792.
KEGG	pae:PA0555.
PATRIC	19835372. VBIPseAer58763_0587.
Organism-specific databases
PseudoCAP	PA0555.
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227792.
KO	K01624.
OMA	EWLKIIN.
ProtClustDB	PRK09196.
Enzyme and pathway databases
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006412. Fruct_bisP_Calv. 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. TIGR01521. FruBisAldo_II_B. 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_PSEAE

Accession

Primary (citable) accession number: Q9I5Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program