Q5XA12 (ALF_STRP6) 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:	M6_Spy1616

Organism

Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) [Complete proteome] [HAMAP]

Taxonomic identifier

286636 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pyogenes › Streptococcus pyogenes serotype M6

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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 Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 293	292	Fructose-bisphosphate aldolase		PRO_0000178749
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)
	Q5XA12 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 29B9DF899FCCA085	FASTA	293	31,136
	10 20 30 40 50 60 MAIVSAEKFV QAARENGYAV GGFNTNNLEW TQAILRAAEA KQAPVLIQTS MGAAKYMGGY 70 80 90 100 110 120 KVCQSLITNL VESMGITVPV AIHLDHGHYG DALECIEVGY TSIMFDGSHL PVEENLAKTA 130 140 150 160 170 180 EVVKIAHAKG VSVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP 190 200 210 220 230 240 YPENWEGLAL DHLEKLTAAV PGFPIVLHGG SGIPDDQIKE AIRLGVAKVN VNTESQIAFS 250 260 270 280 290 NATREFARNY EANEAEYDGK KLFDPRKFLA PGMKAVQGAV EERIDVFGSA NKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain." Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M. J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-946 / MGAS10394.
[2]	"Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins." Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A. Submitted (MAY-2000) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12; 15-36; 130-150; 196-219; 224-244 AND 284-293, MASS SPECTROMETRY. Strain: JRS4 / Serotype M6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000003 Genomic DNA. Translation: AAT87751.1.
RefSeq	YP_060934.1. NC_006086.1.
3D structure databases
ProteinModelPortal	Q5XA12.
ModBase	Search...
Protein-protein interaction databases
STRING	286636.M6_Spy1616.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT87751; AAT87751; M6_Spy1616.
GeneID	2941804.
KEGG	spa:M6_Spy1616.
PATRIC	19725498. VBIStrPyo30273_1680.
Organism-specific databases
CMR	Search...
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_STRP6

Accession

Primary (citable) accession number: Q5XA12
Secondary accession number(s): P82486

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program