Q5HM97 (ALF2_STAEQ) 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:	fbaA
Ordered Locus Names:	SERP1732

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus epidermidis

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-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 – 286	286	Fructose-bisphosphate aldolase		PRO_0000178742
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)
	Q5HM97 [UniParc]. Last modified February 15, 2005. 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]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000029 Genomic DNA. Translation: AAW55054.1.
RefSeq	YP_189296.1. NC_002976.3.
3D structure databases
ProteinModelPortal	Q5HM97.
ModBase	Search...
Protein-protein interaction databases
STRING	176279.SERP1732.
Proteomic databases
PRIDE	Q5HM97.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW55054; AAW55054; SERP1732.
GeneID	3242721.
KEGG	ser:SERP1732.
PATRIC	19614385. VBIStaEpi130894_1691.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227793.
KO	K01624.
OMA	AIKETVI.
ProtClustDB	PRK08610.
Enzyme and pathway databases
BioCyc	SEPI176279:GJJB-1801-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. False negative. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF2_STAEQ

Accession

Primary (citable) accession number: Q5HM97

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program