Q59101 (ALF2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase, plasmid
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13

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

Gene names

Name:	cbbAP
Ordered Locus Names:	PHG416

Encoded on

Plasmid megaplasmid pHG1

Organism

Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus necator

Protein attributes

Sequence length	345 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 biosynthesis; Calvin cycle. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homodimer By similarity.
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
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway reductive pentose-phosphate cycle 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 – 345	345	Fructose-bisphosphate aldolase, plasmid		PRO_0000178728
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
Experimental info
	Sequence conflict	285	1	T → I in AAC43448. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q59101 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: B5E2CBB6200388B7	FASTA	345	37,412
	10 20 30 40 50 60 MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAEE TDSPVILQAS AGARKYAGEA 70 80 90 100 110 120 YLRHMVLAAA ETHPDIPIVL HQDHGSSPAV CQASIRSGFT SVMMDGSLRE DMKTPSDYDY 130 140 150 160 170 180 NVDVTRRVCE MAHAVGVSVE GELGCLGSLE TGQAGEEDGV GAAGTLSHDM MLTDPAQARD 190 200 210 220 230 240 FVARTGVDAL AIAIGTSHGA YKFSRKPTGD ILAIDRIREI HEQIPDTHLV MHGSSSVPQE 250 260 270 280 290 300 WLEIIRQYGG DIKETYGVPV EEILRGIKTG VRKVNIDTDI RLAMTGAIRK SLAEDRSEFD 310 320 330 340 PRKALLAAKK GARSVVKLRF EAFGCAGQAS KIKPIAMEQL AQWYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the genes forming the distal parts of the two cbb CO2 fixation operons from Alcaligenes eutrophus." Schaeferfohann J., Yoo J.-G., Bowien B. Arch. Microbiol. 163:291-299(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis." Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G. J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12423 Genomic DNA. Translation: AAC43448.1. AY305378 Genomic DNA. Translation: AAP86165.1.
PIR	I39555.
RefSeq	NP_943051.1. NC_005241.1.
3D structure databases
ProteinModelPortal	Q59101.
ModBase	Search...
Protein-protein interaction databases
STRING	381666.PHG416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2656760.
KEGG	reh:PHG416.
PATRIC	35229344. VBIRalEut6770_0344.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
HOGENOM	HOG000227792.
KO	K01624.
OMA	CRERFEQ.
ProtClustDB	PRK13399.
Enzyme and pathway databases
BioCyc	CNEC381666:GJUJ-6690-MONOMER.
UniPathway	UPA00109; UER00183. UPA00116.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006412. Fruct_bisP_Calv. 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. 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_CUPNH

Accession

Primary (citable) accession number: Q59101
Secondary accession number(s): Q7WWS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program