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Protein

Fructose-bisphosphate aldolase 2

Gene

cfxB

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: Annotation score: 4 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

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

BioCyciRETL1328306-WGS:GSTH-5054-MONOMER.
UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 2 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase II
Gene namesi
Name:cfxB
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Fructose-bisphosphate aldolase 2PRO_0000178733Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP29271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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.

P29271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS
60 70 80 90 100
RGARSYANDI MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT
110 120 130 140 150
SVMMDGSLKA DAKTPADYDY NVDITARVSH MAHWVGASVE GELGVLGSLE
160 170 180 190 200
TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD FVKKTQVDAL AIACGTSHGA
210 220 230 240 250
YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE LQDIINAFGG
260 270 280 290 300
AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD
310 320 330 340 350
PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA

PKTA
Length:354
Mass (Da):38,269
Last modified:December 1, 1992 - v1
Checksum:i9F547E84FC72ACF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68914 Genomic DNA. Translation: AAA26157.1.
PIRiD41080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68914 Genomic DNA. Translation: AAA26157.1.
PIRiD41080.

3D structure databases

ProteinModelPortaliP29271.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
UPA00116.
BioCyciRETL1328306-WGS:GSTH-5054-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

  1. "Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides."
    Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.
    J. Biol. Chem. 266:20447-20452(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiALF2_RHOSH
AccessioniPrimary (citable) accession number: P29271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.

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.