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Q59101 (ALF2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 onPlasmid megaplasmid pHG1
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceInferred 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 processCalvin cycle
Glycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Fructose-bisphosphate aldolase, plasmid
PRO_0000178728

Regions

Region233 – 2353Dihydroxyacetone phosphate binding By similarity
Region275 – 2784Dihydroxyacetone phosphate binding By similarity

Sites

Active site831Proton donor By similarity
Metal binding841Zinc 1; catalytic By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1421Zinc 2 By similarity
Metal binding1981Zinc 1; catalytic By similarity
Metal binding2321Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1991Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict2851T → I in AAC43448. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59101 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: B5E2CBB6200388B7

FASTA34537,412
        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 

« Hide

References

« Hide '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.
PIRI39555.
RefSeqNP_943051.1. NC_005241.1.

3D structure databases

ProteinModelPortalQ59101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.PHG416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2656760.
KEGGreh:PHG416.
PATRIC35229344. VBIRalEut6770_0344.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227792.
KOK01624.
OMAQGYAVPA.
OrthoDBEOG6HXJ7B.
ProtClustDBPRK13399.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-6690-MONOMER.
UniPathwayUPA00109; UER00183.
UPA00116.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF2_CUPNH
AccessionPrimary (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: November 13, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways