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Protein

Fructose-bisphosphate aldolase 1

Gene

cfxA

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

  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

UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Fructose-bisphosphate aldolase 1PRO_0000178731Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP27995.
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.

P27995-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALITLRQLL DHAAERLQGY GVPAFNINNM EQGLAILAAA RACDAPVIAS
60 70 80 90 100
RGARSYAGDI MLRHIVEALA EMYPQIPICL HQDHGNNEAT CLSAIRHGFT
110 120 130 140 150
SVMMDGSLQA DMKTVASYDY NVDITRRVTD AAHWVGASVE GELGVLGSLE
160 170 180 190 200
KGEAEAEDGS GAEGKLDHSQ MLTDPDQAVE FVQATRVDAL AIAMGTSHGA
210 220 230 240 250
YKFSRKPDGE ILAMRVIEEI HARLPATHLV MHGSSSVAAR LQDLINAHGA
260 270 280 290 300
DMPQTYGVPV EEIERGIRHG VRKVNIDTDC RMALTGQFRK VAMESPKEFD
310 320 330 340 350
ARKFMIPAMK EMEALVRDRF ERFGTAGNAS KITVIPMDDM AKRYASGALD

PAVATAKAA
Length:359
Mass (Da):38,872
Last modified:August 1, 1992 - v1
Checksum:i6A898301D5A2F1ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64624 Genomic DNA. Translation: AAA26114.1.
PIRiB40767. ADRFAS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64624 Genomic DNA. Translation: AAA26114.1.
PIRiB40767. ADRFAS.

3D structure databases

ProteinModelPortaliP27995.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
UPA00116.

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. "Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides."
    Gibson J.L., Falcone D.L., Tabita F.R.
    J. Biol. Chem. 266:14646-14653(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiALF1_RHOSH
AccessioniPrimary (citable) accession number: P27995
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 70 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 I ribulose-bisphosphate carboxylase operon, which predominates when carbon dioxide is limiting.

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.