Reviewed, UniProtKB/Swiss-Prot P29271 (ALF2_RHOSH)

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:

cfxB

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
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.
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	Metal-binding 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 – 354	354	Fructose-bisphosphate aldolase 2		PRO_0000178733
Regions
	Region	233 – 235	3	Dihydroxyacetone phosphate binding By similarity
	Region	275 – 278	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	83	1	Proton donor By similarity
	Metal binding	84	1	Zinc 1; catalytic By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	142	1	Zinc 2 By similarity
	Metal binding	198	1	Zinc 1; catalytic By similarity
	Metal binding	232	1	Zinc 1; catalytic By similarity
	Binding site	50	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	199	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29271-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 9F547E84FC72ACF5	FASTA	354	38,269
	10 20 30 40 50 60 MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS RGARSYANDI 70 80 90 100 110 120 MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT SVMMDGSLKA DAKTPADYDY 130 140 150 160 170 180 NVDITARVSH MAHWVGASVE GELGVLGSLE TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD 190 200 210 220 230 240 FVKKTQVDAL AIACGTSHGA YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE 250 260 270 280 290 300 LQDIINAFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD 310 320 330 340 350 PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA PKTA

References

[1]

"Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides." Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R. J. Biol. Chem. 266:20447-20452(1991) [PubMed: 1939098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M68914 Genomic DNA. Translation: AAA26157.1.
PIR	D41080.
3D structure databases
HSSP	HSSP built from PDB template 1GVF based on UniProtKB P42908.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.2.13. 2796.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006412. Fruct_bisP_Calv. 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.
ProDom	PD002376. K_bP_aldolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00167. cbbA. 1 hit. TIGR01521. FruBisAldo_II_B. 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

ALF2_RHOSH

Accession

Primary (citable) accession number: P29271

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 50 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)