Reviewed, UniProtKB/Swiss-Prot Q6GEV0 (ALF2_STAAR)

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:	fbaA
Ordered Locus Names:	SAR2213

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: InterPro
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: InterPro 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 – 286	286	Fructose-bisphosphate aldolase		PRO_0000178738
Regions
	Region	210 – 212	3	Dihydroxyacetone phosphate binding By similarity
	Region	231 – 234	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	107	1	Zinc 2 By similarity
	Metal binding	137	1	Zinc 2 By similarity
	Metal binding	181	1	Zinc 1; catalytic By similarity
	Metal binding	209	1	Zinc 1; catalytic By similarity
	Binding site	50	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	182	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GEV0-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 7A5FD0EBD48283D9	FASTA	286	30,836
	10 20 30 40 50 60 MPLVSMKEML IDAKENGYAV GQYNINNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF 70 80 90 100 110 120 YTIVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVATT 130 140 150 160 170 180 KKVVEYAHEK GVSVEAELGT VGGQEDDVVA DGIIYADPKE CQELVEKTGI DALAPALGSV 190 200 210 220 230 240 HGPYKGEPKL GFKEMEEIGL STGLPLVLHG GTGIPTKDIQ KAIPFGTAKI NVNTENQIAS 250 260 270 280 AKAVRDVLNN DKEVYDPRKY LGPAREAIKE TVKGKIKEFG TSNRAK

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571856 Genomic DNA. Translation: CAG41194.1.
RefSeq	YP_041573.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2860015.
GenomeReviews	Gene locus SAR2213 in contig BX571856_GR.
KEGG	sar:SAR2213.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6GEV0.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR2213-MON.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR011289. Fruc_bis_ald_. IPR000771. K_bP_aldolase. [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.
ProDom	PD002376. K_bP_aldolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00167. cbbA. 1 hit. TIGR01859. fruc_bis_ald_. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. False negative. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF2_STAAR

Accession

Primary (citable) accession number: Q6GEV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 26 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)