Reviewed, UniProtKB/Swiss-Prot Q8CNI3 (ALF2_STAES)

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:	SE_1723

Organism

Staphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]

Taxonomic identifier

176280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	286 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
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 286	286	Fructose-bisphosphate aldolase		PRO_0000178741
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)
	Q8CNI3-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D11CBF24BAE3B4E6	FASTA	286	30,883
	10 20 30 40 50 60 MPLVSMKEML IDAKENGYAV GQYNLNNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF 70 80 90 100 110 120 YTVVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVEIT 130 140 150 160 170 180 SKVVEYAHDR GVSVEAELGT VGGQEDDVVA DGVIYADPKE CQELVEKTGI DTLAPALGSV 190 200 210 220 230 240 HGPYKGEPKL GFKEMEEIGA STGLPLVLHG GTGIPTKDIQ KAIPYGTAKI NVNTENQIAS 250 260 270 280 AKAVREVLNN DKDVYDPRKY LGPAREAIKE TVKGKIREFG TSNRAK

References

[1]

"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015929 Genomic DNA. Translation: AAO05322.1.
RefSeq	NP_765278.1.
3D structure databases
SMR	Q8CNI3. Positions 3-285.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CNI3.
Genome annotation databases
GeneID	1057228.
GenomeReviews	Gene locus SE_1723 in contig AE015929_GR.
KEGG	sep:SE1723.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HBG327581.
OMA	RTGIDCL.
PhylomeDB	Q8CNI3.
Enzyme and pathway databases
BioCyc	SEPI176280:SE_1723-MONOMER.
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. False negative. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF2_STAES

Accession

Primary (citable) accession number: Q8CNI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 45 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)