Reviewed, UniProtKB/Swiss-Prot Q59100 (ALF1_RALEH)

Names and origin

Protein names

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

Gene names

Name:	cbbAC
Synonyms:	cbbA2
Ordered Locus Names:	H16_B1384

Organism

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

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	345 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 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
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 – 345	345	Fructose-bisphosphate aldolase, chromosomal		PRO_0000178727
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	19	1	G → D in AAC43445. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q59100-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DABCBE4C408F2B4B	FASTA	345	37,397
	10 20 30 40 50 60 MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAQE TDSPVILQAS AGARKYAGEA 70 80 90 100 110 120 YLRHMVLAAA ETHPDIPIVL HQDHGSSPAI CQASIRSGFT SVMMDGSLRE DMKTPSDYDY 130 140 150 160 170 180 NVEVTRRVCE MAHAIGVSVE GELGCLGSLE TGQAGEEDGV GAAGTLSHDM MLTDPAQARD 190 200 210 220 230 240 FVARTGVDAL AIAIGTSHGA YKFSRKPTGD ILAMDRIREI HEQIPDTHLV MHGSSSVPQE 250 260 270 280 290 300 WLEIIRQYGG DIKETYGVPV EEILRGIKMG VRKVNIDTDI RLAMTGAIRK SLSDDRSEFD 310 320 330 340 PRKALLAAKK GARSVVKLRF EAFGCAGQAS RIKPVPLERV AKLYS

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: 7763137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U12422 Genomic DNA. Translation: AAC43445.1. AM260480 Genomic DNA. Translation: CAJ96173.1.
PIR	I39552.
RefSeq	YP_840903.1.
3D structure databases
HSSP	HSSP built from PDB template 1GVF based on UniProtKB P42908.
ModBase	Search...
Protein-protein interaction databases
STRING	Q59100.
Genome annotation databases
GeneID	4455910.
GenomeReviews	Gene locus H16_B1384 in contig AM260480_GR.
KEGG	reh:H16_B1384.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q59100.
OMA	ASHEEFE.
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

ALF1_RALEH

Accession

Primary (citable) accession number: Q59100
Secondary accession number(s): Q0K1F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)