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Protein

Fructose-bisphosphate aldolase, plasmid

Gene

cbbAP

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathway: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Pathway: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi)
  3. no protein annotated in this organism
  4. Fructose-bisphosphate aldolase, chromosomal (cbbAC), Fructose-bisphosphate aldolase, plasmid (cbbAP)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Glyceraldehyde 3-phosphateBy similarity
Active sitei83 – 831Proton donorBy similarity
Metal bindingi84 – 841Zinc 1; catalyticBy similarity
Metal bindingi105 – 1051Zinc 2By similarity
Metal bindingi142 – 1421Zinc 2By similarity
Metal bindingi198 – 1981Zinc 1; catalyticBy similarity
Binding sitei199 – 1991Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi232 – 2321Zinc 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Calvin cycle, Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-6690-MONOMER.
UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, plasmid (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:cbbAP
Ordered Locus Names:PHG416
Encoded oniPlasmid megaplasmid pHG10 Publication
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210 Componenti: Plasmid megaplasmid pHG1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Fructose-bisphosphate aldolase, plasmidPRO_0000178728Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi381666.H16_B1384.

Structurei

3D structure databases

ProteinModelPortaliQ59101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni233 – 2353Dihydroxyacetone phosphate bindingBy similarity
Regioni275 – 2784Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiDLCRERF.
OrthoDBiEOG6HXJ7B.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAEE TDSPVILQAS
60 70 80 90 100
AGARKYAGEA YLRHMVLAAA ETHPDIPIVL HQDHGSSPAV CQASIRSGFT
110 120 130 140 150
SVMMDGSLRE DMKTPSDYDY NVDVTRRVCE MAHAVGVSVE GELGCLGSLE
160 170 180 190 200
TGQAGEEDGV GAAGTLSHDM MLTDPAQARD FVARTGVDAL AIAIGTSHGA
210 220 230 240 250
YKFSRKPTGD ILAIDRIREI HEQIPDTHLV MHGSSSVPQE WLEIIRQYGG
260 270 280 290 300
DIKETYGVPV EEILRGIKTG VRKVNIDTDI RLAMTGAIRK SLAEDRSEFD
310 320 330 340
PRKALLAAKK GARSVVKLRF EAFGCAGQAS KIKPIAMEQL AQWYR
Length:345
Mass (Da):37,412
Last modified:January 4, 2005 - v2
Checksum:iB5E2CBB6200388B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851T → I in AAC43448 (PubMed:7763137).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12423 Genomic DNA. Translation: AAC43448.1.
AY305378 Genomic DNA. Translation: AAP86165.1.
PIRiI39555.
RefSeqiNP_943051.1. NC_005241.1.
WP_011154328.1. NC_005241.1.
YP_009074644.1. NG_034711.1.

Genome annotation databases

EnsemblBacteriaiAAP86165; AAP86165; PHG416.
GeneIDi2656760.
KEGGireh:PHG416.
PATRICi35229344. VBIRalEut6770_0344.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12423 Genomic DNA. Translation: AAC43448.1.
AY305378 Genomic DNA. Translation: AAP86165.1.
PIRiI39555.
RefSeqiNP_943051.1. NC_005241.1.
WP_011154328.1. NC_005241.1.
YP_009074644.1. NG_034711.1.

3D structure databases

ProteinModelPortaliQ59101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_B1384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP86165; AAP86165; PHG416.
GeneIDi2656760.
KEGGireh:PHG416.
PATRICi35229344. VBIRalEut6770_0344.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiDLCRERF.
OrthoDBiEOG6HXJ7B.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
UPA00116.
BioCyciCNEC381666:GJUJ-6690-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiALF2_CUPNH
AccessioniPrimary (citable) accession number: Q59101
Secondary accession number(s): Q7WWS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 4, 2005
Last modified: June 24, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.