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Q59100 (ALF1_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

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
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: 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, chromosomal
PRO_0000178727

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 conflict191G → D in AAC43445. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59100 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DABCBE4C408F2B4B

FASTA34537,397
        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

« 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]"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] [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		U12422 Genomic DNA. Translation: AAC43445.1.
AM260480 Genomic DNA. Translation: CAJ96173.1.
PIRI39552.
RefSeqYP_840903.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ59100.
ModBaseSearch...

Protein-protein interaction databases

STRING381666.H16_B1384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ96173; CAJ96173; H16_B1384.
GeneID4455910.
KEGGreh:H16_B1384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227792.
KOK01624.
OMALIIETSE.
ProtClustDBPRK13399.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-5089-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 nameALF1_CUPNH
AccessionPrimary (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: May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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