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Protein

Fructose-bisphosphate aldolase, chromosomal

Gene

cbbAC

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

Pathwayi

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

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
  2. reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Calvin cycle, Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-5089-MONOMER.
UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, chromosomal (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:cbbAC
Synonyms:cbbA2
Ordered Locus Names:H16_B1384
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Fructose-bisphosphate aldolase, chromosomalPRO_0000178727Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi381666.H16_B1384.

Structurei

3D structure databases

ProteinModelPortaliQ59100.
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.
OMAiCRMAMAG.
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.

Q59100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAQE TDSPVILQAS
60 70 80 90 100
AGARKYAGEA YLRHMVLAAA ETHPDIPIVL HQDHGSSPAI CQASIRSGFT
110 120 130 140 150
SVMMDGSLRE DMKTPSDYDY NVEVTRRVCE MAHAIGVSVE GELGCLGSLE
160 170 180 190 200
TGQAGEEDGV GAAGTLSHDM MLTDPAQARD FVARTGVDAL AIAIGTSHGA
210 220 230 240 250
YKFSRKPTGD ILAMDRIREI HEQIPDTHLV MHGSSSVPQE WLEIIRQYGG
260 270 280 290 300
DIKETYGVPV EEILRGIKMG VRKVNIDTDI RLAMTGAIRK SLSDDRSEFD
310 320 330 340
PRKALLAAKK GARSVVKLRF EAFGCAGQAS RIKPVPLERV AKLYS
Length:345
Mass (Da):37,397
Last modified:January 23, 2007 - v2
Checksum:iDABCBE4C408F2B4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → D in AAC43445 (PubMed:7763137).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12422 Genomic DNA. Translation: AAC43445.1.
AM260480 Genomic DNA. Translation: CAJ96173.1.
PIRiI39552.
RefSeqiYP_840903.1. NC_008314.1.

Genome annotation databases

EnsemblBacteriaiCAJ96173; CAJ96173; H16_B1384.
KEGGireh:H16_B1384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12422 Genomic DNA. Translation: AAC43445.1.
AM260480 Genomic DNA. Translation: CAJ96173.1.
PIRiI39552.
RefSeqiYP_840903.1. NC_008314.1.

3D structure databases

ProteinModelPortaliQ59100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_B1384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ96173; CAJ96173; H16_B1384.
KEGGireh:H16_B1384.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiCRMAMAG.
OrthoDBiEOG6HXJ7B.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
UPA00116.
BioCyciCNEC381666:GJUJ-5089-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiALF1_CUPNH
AccessioniPrimary (citable) accession number: Q59100
Secondary accession number(s): Q0K1F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 93 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, 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.