Q89AB6 (ALF_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase class 2
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13

Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II

Gene names

Name:	fbaA
Synonyms:	fba
Ordered Locus Names:	bbp_401

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	359 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	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 – 359	359	Fructose-bisphosphate aldolase class 2		PRO_0000178710
Regions
	Region	266 – 268	3	Dihydroxyacetone phosphate binding By similarity
	Region	287 – 290	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	110	1	Proton donor By similarity
	Metal binding	111	1	Zinc 1; catalytic By similarity
	Metal binding	145	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 2 By similarity
	Metal binding	227	1	Zinc 1; catalytic By similarity
	Metal binding	265	1	Zinc 1; catalytic By similarity
	Binding site	62	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	228	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AB6 [UniParc]. Last modified May 30, 2003. Version 1. Checksum: 49DE95BCADB14B5B	FASTA	359	40,487
	10 20 30 40 50 60 MCNILNKIKP GVITGNEALK LFKIAKKNHF AIPAINCINT DSINIVLETA KKAKSPVIIQ 70 80 90 100 110 120 FSYGGSNFIS GPGLTTNILH KKAIIGALSG ANHVHIMAKH YNVPVILHTD HCNKNMLPWI 130 140 150 160 170 180 DELINVGTKH FKTYNKPLFT SHMIDLSNEK LDYNINICSK YLEKMRKINM LLEIELGCTG 190 200 210 220 230 240 GEEDGINNTK INKSLLYTQP NEVNYAYERL SSVGPEFIIA ASFGNVHGVY KSGNVRLTPD 250 260 270 280 290 300 ILKKSQNYVS KKHNLSCNPL CFVFHGGSGS SEKDIKKSIK YGVIKMNIDT DIQWATWQGI 310 320 330 340 350 LNFYNKNNKY LHNQIGNLDN ENKPNKKYYD PRTWIRSSQI SVSNHLTKIF RILNSCNTL

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO27113.1.
RefSeq	NP_778008.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AB6.
SMR	Q89AB6. Positions 4-359.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp401.
Proteomic databases
PRIDE	Q89AB6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO27113; AAO27113; bbp_401.
GeneID	1058292.
KEGG	bab:bbp401.
PATRIC	21245605. VBIBucAph80364_0396.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
KO	K01624.
OMA	DYNINIC.
ProtClustDB	PRK09197.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-401-MONOMER.
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006411. Fruct_bisP_bact. 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. TIGR01520. FruBisAldo_II_A. 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_BUCBP

Accession

Primary (citable) accession number: Q89AB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2003
Last sequence update:	May 30, 2003
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program