Reviewed, UniProtKB/Swiss-Prot P50923 (ALF2_RHOCA)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase 2
      Short name=FBP aldolase
      Short name=FBPA
    EC=4.1.2.13
Alternative name(s):
    Fructose-bisphosphate aldolase II
    Fructose-1,6-bisphosphate aldolase

Gene names

Name:	cbbA
Synonyms:	cfxB

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	114 AA.
Sequence status	Fragment.
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 biosynthesis; Calvin cycle. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homodimer By similarity.
Miscellaneous	This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Calvin cycle Glycolysis
Ligand	Zinc
Molecular function	Lyase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle 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 – 114	›114	Fructose-bisphosphate aldolase 2		PRO_0000178732
Regions
	Region	35 – 38	4	Dihydroxyacetone phosphate binding By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P50923-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 18811FF5D217BD92	FASTA	114	12,747
	10 20 30 40 50 60 LQDIINEFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMRMTGQFRR IAEQNKAEFD 70 80 90 100 110 PRKFLKPAMD AMRDLCKARL EAFGTAGHAS KIKVIPMDDM AKRYASGSLA PKTN

References

[1]	Larimer F.W., Lu T.-Y.S., Buley D.M. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11166 / DSM 1710 / IFO 16435 / LMG 2962 / NCIB 8254.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U23145 Genomic DNA. Translation: AAB82047.1.
PIR	T10505.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.2.13. 567.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. 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]
ProDom	PD002376. K_bP_aldolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00602. ALDOLASE_CLASS_II_1. Partial match. PS00806. ALDOLASE_CLASS_II_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALF2_RHOCA

Accession

Primary (citable) accession number: P50923

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 42 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)